Comparative structural analysis of a novel glutathione S-transferase (Atu5508) from Agrobacterium tumefaciens at 2.0 Å resolution

Mickey Kosloff; Gye Won Han; S. Sri Krishna; Robert Schwarzenbacher; Marc Fasnacht; Marc André Elsliger; Polat Abdubek; Sanjay Agarwalla; Eileen Ambing; Tamara Astakhova; Herbert L. Axelrod; Jaume M. Canaves; Dennis Carlton; Hsiu Ju Chiu; Thomas Clayton; Michael DiDonato; Lian Duan; Julie Feuerhelm; Carina Grittini; Slawomir K. Grzechnik; Joanna Hale; Eric Hampton; Justin Haugen; Lukasz Jaroszewski; Kevin K. Jin; Hope Johnson; Heath E. Klock; Mark W. Knuth; Eric Koesema; Andreas Kreusch; Peter Kuhn; Inna Levin; Daniel McMullan; Mitchell D. Miller; Andrew T. Morse; Kin Moy; Edward Nigoghossian; Linda Okach; Silvya Oommachen; Rebecca Page; Jessica Paulsen; Kevin Quijano; Ron Reyes; Christopher L. Rife; Eric Sims; Glen Spraggon; Vandana Sridhar; Raymond C. Stevens; Henry Van Den Bedem; Jeff Velasquez; Aprilfawn White; Guenter Wolf; Qingping Xu; Keith O. Hodgson; John Wooley; Ashley M. Deacon; Adam Godzik; Scott A. Lesley; Ian A. Wilson

doi:10.1002/prot.21130

Comparative structural analysis of a novel glutathione S-transferase (Atu5508) from Agrobacterium tumefaciens at 2.0 Å resolution

Mickey Kosloff, Gye Won Han, S. Sri Krishna, Robert Schwarzenbacher, Marc Fasnacht, Marc André Elsliger, Polat Abdubek, Sanjay Agarwalla, Eileen Ambing, Tamara Astakhova, Herbert L. Axelrod, Jaume M. Canaves, Dennis Carlton, Hsiu Ju Chiu, Thomas Clayton, Michael DiDonato, Lian Duan, Julie Feuerhelm, Carina Grittini, Slawomir K. GrzechnikJoanna Hale, Eric Hampton, Justin Haugen, Lukasz Jaroszewski, Kevin K. Jin, Hope Johnson, Heath E. Klock, Mark W. Knuth, Eric Koesema, Andreas Kreusch, Peter Kuhn, Inna Levin, Daniel McMullan, Mitchell D. Miller, Andrew T. Morse, Kin Moy, Edward Nigoghossian, Linda Okach, Silvya Oommachen, Rebecca Page, Jessica Paulsen, Kevin Quijano, Ron Reyes, Christopher L. Rife, Eric Sims, Glen Spraggon, Vandana Sridhar, Raymond C. Stevens, Henry Van Den Bedem, Jeff Velasquez, Aprilfawn White, Guenter Wolf, Qingping Xu, Keith O. Hodgson, John Wooley, Ashley M. Deacon, Adam Godzik, Scott A. Lesley, Ian A. Wilson

Research output: Contribution to journal › Article › peer-review

Abstract

Glutathione S-transferases (GSTs) comprise a diverse superfamily of enzymes found in organisms from all kingdoms of life. GSTs are involved in diverse processes, notably small-molecule biosynthesis or detoxification, and are frequently also used in protein engineering studies or as biotechnology tools. Here, we report the high-resolution X-ray structure of Atu5508 from the pathogenic soil bacterium Agrobacterium tumefaciens (atGST1). Through use of comparative sequence and structural analysis of the GST superfamily, we identified local sequence and structural signatures, which allowed us to distinguish between different GST classes. This approach enables GST classification based on structure, without requiring additional biochemical or immunological data. Consequently, analysis of the atGST1 crystal structure suggests a new GST class, distinct from previously characterized GSTs, which would make it an attractive target for further biochemical studies.

Original language	English
Pages (from-to)	527-537
Number of pages	11
Journal	Proteins: Structure, Function and Genetics
Volume	65
Issue number	3
DOIs	https://doi.org/10.1002/prot.21130
State	Published - 15 Nov 2006
Externally published	Yes

Keywords

Active site
Consensus sequence
Dimer interface
Glutathione transferase
JCSG
Local structural motif
Specificity
Structural genomics
X-ray crystallography

ASJC Scopus subject areas

Structural Biology
Biochemistry
Molecular Biology

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10.1002/prot.21130

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Kosloff, M., Han, G. W., Sri Krishna, S., Schwarzenbacher, R., Fasnacht, M., Elsliger, M. A., Abdubek, P., Agarwalla, S., Ambing, E., Astakhova, T., Axelrod, H. L., Canaves, J. M., Carlton, D., Chiu, H. J., Clayton, T., DiDonato, M., Duan, L., Feuerhelm, J., Grittini, C., ... Wilson, I. A. (2006). Comparative structural analysis of a novel glutathione S-transferase (Atu5508) from Agrobacterium tumefaciens at 2.0 Å resolution. Proteins: Structure, Function and Genetics, 65(3), 527-537. https://doi.org/10.1002/prot.21130

@article{263167bdef6643f29e3c93fe969b0714,

title = "Comparative structural analysis of a novel glutathione S-transferase (Atu5508) from Agrobacterium tumefaciens at 2.0 {\AA} resolution",

abstract = "Glutathione S-transferases (GSTs) comprise a diverse superfamily of enzymes found in organisms from all kingdoms of life. GSTs are involved in diverse processes, notably small-molecule biosynthesis or detoxification, and are frequently also used in protein engineering studies or as biotechnology tools. Here, we report the high-resolution X-ray structure of Atu5508 from the pathogenic soil bacterium Agrobacterium tumefaciens (atGST1). Through use of comparative sequence and structural analysis of the GST superfamily, we identified local sequence and structural signatures, which allowed us to distinguish between different GST classes. This approach enables GST classification based on structure, without requiring additional biochemical or immunological data. Consequently, analysis of the atGST1 crystal structure suggests a new GST class, distinct from previously characterized GSTs, which would make it an attractive target for further biochemical studies.",

keywords = "Active site, Consensus sequence, Dimer interface, Glutathione transferase, JCSG, Local structural motif, Specificity, Structural genomics, X-ray crystallography",

author = "Mickey Kosloff and Han, {Gye Won} and {Sri Krishna}, S. and Robert Schwarzenbacher and Marc Fasnacht and Elsliger, {Marc Andr{\'e}} and Polat Abdubek and Sanjay Agarwalla and Eileen Ambing and Tamara Astakhova and Axelrod, {Herbert L.} and Canaves, {Jaume M.} and Dennis Carlton and Chiu, {Hsiu Ju} and Thomas Clayton and Michael DiDonato and Lian Duan and Julie Feuerhelm and Carina Grittini and Grzechnik, {Slawomir K.} and Joanna Hale and Eric Hampton and Justin Haugen and Lukasz Jaroszewski and Jin, {Kevin K.} and Hope Johnson and Klock, {Heath E.} and Knuth, {Mark W.} and Eric Koesema and Andreas Kreusch and Peter Kuhn and Inna Levin and Daniel McMullan and Miller, {Mitchell D.} and Morse, {Andrew T.} and Kin Moy and Edward Nigoghossian and Linda Okach and Silvya Oommachen and Rebecca Page and Jessica Paulsen and Kevin Quijano and Ron Reyes and Rife, {Christopher L.} and Eric Sims and Glen Spraggon and Vandana Sridhar and Stevens, {Raymond C.} and {Van Den Bedem}, Henry and Jeff Velasquez and Aprilfawn White and Guenter Wolf and Qingping Xu and Hodgson, {Keith O.} and John Wooley and Deacon, {Ashley M.} and Adam Godzik and Lesley, {Scott A.} and Wilson, {Ian A.}",

year = "2006",

month = nov,

day = "15",

doi = "10.1002/prot.21130",

language = "English",

volume = "65",

pages = "527--537",

journal = "Proteins: Structure, Function and Bioinformatics",

issn = "0887-3585",

publisher = "Wiley-Liss Inc.",

number = "3",

}

Kosloff, M, Han, GW, Sri Krishna, S, Schwarzenbacher, R, Fasnacht, M, Elsliger, MA, Abdubek, P, Agarwalla, S, Ambing, E, Astakhova, T, Axelrod, HL, Canaves, JM, Carlton, D, Chiu, HJ, Clayton, T, DiDonato, M, Duan, L, Feuerhelm, J, Grittini, C, Grzechnik, SK, Hale, J, Hampton, E, Haugen, J, Jaroszewski, L, Jin, KK, Johnson, H, Klock, HE, Knuth, MW, Koesema, E, Kreusch, A, Kuhn, P, Levin, I, McMullan, D, Miller, MD, Morse, AT, Moy, K, Nigoghossian, E, Okach, L, Oommachen, S, Page, R, Paulsen, J, Quijano, K, Reyes, R, Rife, CL, Sims, E, Spraggon, G, Sridhar, V, Stevens, RC, Van Den Bedem, H, Velasquez, J, White, A, Wolf, G, Xu, Q, Hodgson, KO, Wooley, J, Deacon, AM, Godzik, A, Lesley, SA & Wilson, IA 2006, 'Comparative structural analysis of a novel glutathione S-transferase (Atu5508) from Agrobacterium tumefaciens at 2.0 Å resolution', Proteins: Structure, Function and Genetics, vol. 65, no. 3, pp. 527-537. https://doi.org/10.1002/prot.21130

TY - JOUR

T1 - Comparative structural analysis of a novel glutathione S-transferase (Atu5508) from Agrobacterium tumefaciens at 2.0 Å resolution

AU - Kosloff, Mickey

AU - Han, Gye Won

AU - Sri Krishna, S.

AU - Schwarzenbacher, Robert

AU - Fasnacht, Marc

AU - Elsliger, Marc André

AU - Abdubek, Polat

AU - Agarwalla, Sanjay

AU - Ambing, Eileen

AU - Astakhova, Tamara

AU - Axelrod, Herbert L.

AU - Canaves, Jaume M.

AU - Carlton, Dennis

AU - Chiu, Hsiu Ju

AU - Clayton, Thomas

AU - DiDonato, Michael

AU - Duan, Lian

AU - Feuerhelm, Julie

AU - Grittini, Carina

AU - Grzechnik, Slawomir K.

AU - Hale, Joanna

AU - Hampton, Eric

AU - Haugen, Justin

AU - Jaroszewski, Lukasz

AU - Jin, Kevin K.

AU - Johnson, Hope

AU - Klock, Heath E.

AU - Knuth, Mark W.

AU - Koesema, Eric

AU - Kreusch, Andreas

AU - Kuhn, Peter

AU - Levin, Inna

AU - McMullan, Daniel

AU - Miller, Mitchell D.

AU - Morse, Andrew T.

AU - Moy, Kin

AU - Nigoghossian, Edward

AU - Okach, Linda

AU - Oommachen, Silvya

AU - Page, Rebecca

AU - Paulsen, Jessica

AU - Quijano, Kevin

AU - Reyes, Ron

AU - Rife, Christopher L.

AU - Sims, Eric

AU - Spraggon, Glen

AU - Sridhar, Vandana

AU - Stevens, Raymond C.

AU - Van Den Bedem, Henry

AU - Velasquez, Jeff

AU - White, Aprilfawn

AU - Wolf, Guenter

AU - Xu, Qingping

AU - Hodgson, Keith O.

AU - Wooley, John

AU - Deacon, Ashley M.

AU - Godzik, Adam

AU - Lesley, Scott A.

AU - Wilson, Ian A.

PY - 2006/11/15

Y1 - 2006/11/15

N2 - Glutathione S-transferases (GSTs) comprise a diverse superfamily of enzymes found in organisms from all kingdoms of life. GSTs are involved in diverse processes, notably small-molecule biosynthesis or detoxification, and are frequently also used in protein engineering studies or as biotechnology tools. Here, we report the high-resolution X-ray structure of Atu5508 from the pathogenic soil bacterium Agrobacterium tumefaciens (atGST1). Through use of comparative sequence and structural analysis of the GST superfamily, we identified local sequence and structural signatures, which allowed us to distinguish between different GST classes. This approach enables GST classification based on structure, without requiring additional biochemical or immunological data. Consequently, analysis of the atGST1 crystal structure suggests a new GST class, distinct from previously characterized GSTs, which would make it an attractive target for further biochemical studies.

AB - Glutathione S-transferases (GSTs) comprise a diverse superfamily of enzymes found in organisms from all kingdoms of life. GSTs are involved in diverse processes, notably small-molecule biosynthesis or detoxification, and are frequently also used in protein engineering studies or as biotechnology tools. Here, we report the high-resolution X-ray structure of Atu5508 from the pathogenic soil bacterium Agrobacterium tumefaciens (atGST1). Through use of comparative sequence and structural analysis of the GST superfamily, we identified local sequence and structural signatures, which allowed us to distinguish between different GST classes. This approach enables GST classification based on structure, without requiring additional biochemical or immunological data. Consequently, analysis of the atGST1 crystal structure suggests a new GST class, distinct from previously characterized GSTs, which would make it an attractive target for further biochemical studies.

KW - Active site

KW - Consensus sequence

KW - Dimer interface

KW - Glutathione transferase

KW - JCSG

KW - Local structural motif

KW - Specificity

KW - Structural genomics

KW - X-ray crystallography

UR - http://www.scopus.com/inward/record.url?scp=33750178803&partnerID=8YFLogxK

U2 - 10.1002/prot.21130

DO - 10.1002/prot.21130

M3 - Article

C2 - 16988933

AN - SCOPUS:33750178803

SN - 0887-3585

VL - 65

SP - 527

EP - 537

JO - Proteins: Structure, Function and Bioinformatics

JF - Proteins: Structure, Function and Bioinformatics

IS - 3

ER -

Comparative structural analysis of a novel glutathione S-transferase (Atu5508) from Agrobacterium tumefaciens at 2.0 Å resolution

Abstract

Keywords

ASJC Scopus subject areas

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