2fno: Difference between revisions

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New page: left|200px<br /><applet load="2fno" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fno, resolution 2.000Å" /> '''Crystal structure o...
 
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[[Image:2fno.gif|left|200px]]<br /><applet load="2fno" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2fno.gif|left|200px]]<br /><applet load="2fno" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2fno, resolution 2.000&Aring;" />
caption="2fno, resolution 2.000&Aring;" />
'''Crystal structure of Putative glutathione S-transferase (15162326) from AGROBACTERIUM TUMEFACIENS at 2.00 A resolution'''<br />
'''Crystal structure of Putative glutathione S-transferase (15162326) from AGROBACTERIUM TUMEFACIENS at 2.00 A resolution'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
2FNO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens_str._c58 Agrobacterium tumefaciens str. c58] with SCN as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1ZGM. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FNO OCA].  
2FNO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens_str._c58 Agrobacterium tumefaciens str. c58] with <scene name='pdbligand=SCN:'>SCN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1ZGM. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FNO OCA].  


==Reference==
==Reference==
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[[Category: Agrobacterium tumefaciens str. c58]]
[[Category: Agrobacterium tumefaciens str. c58]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: JCSG, Joint.Center.for.Structural.Genomics.]]
[[Category: JCSG, Joint Center for Structural Genomics.]]
[[Category: SCN]]
[[Category: SCN]]
[[Category: 15162326]]
[[Category: 15162326]]
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[[Category: structural genomics]]
[[Category: structural genomics]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:15 2008''

Revision as of 18:23, 21 February 2008

File:2fno.gif


2fno, resolution 2.000Å

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Crystal structure of Putative glutathione S-transferase (15162326) from AGROBACTERIUM TUMEFACIENS at 2.00 A resolution

OverviewOverview

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.

About this StructureAbout this Structure

2FNO is a Single protein structure of sequence from Agrobacterium tumefaciens str. c58 with as ligand. This structure supersedes the now removed PDB entry 1ZGM. Full crystallographic information is available from OCA.

ReferenceReference

Comparative structural analysis of a novel glutathioneS-transferase (ATU5508) from Agrobacterium tumefaciens at 2.0 A resolution., Kosloff M, Han GW, Krishna SS, 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, Proteins. 2006 Nov 15;65(3):527-37. PMID:16988933

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