1rw1: Difference between revisions

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New page: left|200px<br /><applet load="1rw1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rw1, resolution 1.02Å" /> '''YFFB (PA3664) PROTEI...
 
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[[Image:1rw1.gif|left|200px]]<br /><applet load="1rw1" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1rw1.gif|left|200px]]<br /><applet load="1rw1" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1rw1, resolution 1.02&Aring;" />
caption="1rw1, resolution 1.02&Aring;" />
'''YFFB (PA3664) PROTEIN'''<br />
'''YFFB (PA3664) PROTEIN'''<br />


==Overview==
==Overview==
BACKGROUND: The yffB (PA3664) gene of Pseudomonas aeruginosa encodes an, uncharacterized protein of 13 kDa molecular weight with a marginal, sequence similarity to arsenate reductase from Escherichia coli. The, crystal structure determination of YffB was undertaken as part of a, structural genomics effort in order to assist with the functional, assignment of the protein. RESULTS: The structure was determined at 1.0 A, resolution by single-wavelength anomalous diffraction. The fold is very, similar to that of arsenate reductase, which is an extension of the, thioredoxin fold. CONCLUSION: Given the conservation of the functionally, important residues and the ability to bind glutathione, YffB is likely to, function as a GSH-dependent thiol reductase.
BACKGROUND: The yffB (PA3664) gene of Pseudomonas aeruginosa encodes an uncharacterized protein of 13 kDa molecular weight with a marginal sequence similarity to arsenate reductase from Escherichia coli. The crystal structure determination of YffB was undertaken as part of a structural genomics effort in order to assist with the functional assignment of the protein. RESULTS: The structure was determined at 1.0 A resolution by single-wavelength anomalous diffraction. The fold is very similar to that of arsenate reductase, which is an extension of the thioredoxin fold. CONCLUSION: Given the conservation of the functionally important residues and the ability to bind glutathione, YffB is likely to function as a GSH-dependent thiol reductase.


==About this Structure==
==About this Structure==
1RW1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_pao1 Pseudomonas aeruginosa pao1] with IPA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RW1 OCA].  
1RW1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_pao1 Pseudomonas aeruginosa pao1] with <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RW1 OCA].  


==Reference==
==Reference==
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[[Category: Doseeva, V.]]
[[Category: Doseeva, V.]]
[[Category: Galkin, A.]]
[[Category: Galkin, A.]]
[[Category: Gilliland, G.L.]]
[[Category: Gilliland, G L.]]
[[Category: Herzberg, O.]]
[[Category: Herzberg, O.]]
[[Category: Obmolova, G.]]
[[Category: Obmolova, G.]]
[[Category: Pullalarevu, S.]]
[[Category: Pullalarevu, S.]]
[[Category: S2F, Structure.2.Function.Project.]]
[[Category: S2F, Structure 2.Function Project.]]
[[Category: Teplyakov, A.]]
[[Category: Teplyakov, A.]]
[[Category: IPA]]
[[Category: IPA]]
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[[Category: thioredoxin fold]]
[[Category: thioredoxin fold]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:23:13 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:06 2008''

Revision as of 15:55, 21 February 2008

File:1rw1.gif


1rw1, resolution 1.02Å

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YFFB (PA3664) PROTEIN

OverviewOverview

BACKGROUND: The yffB (PA3664) gene of Pseudomonas aeruginosa encodes an uncharacterized protein of 13 kDa molecular weight with a marginal sequence similarity to arsenate reductase from Escherichia coli. The crystal structure determination of YffB was undertaken as part of a structural genomics effort in order to assist with the functional assignment of the protein. RESULTS: The structure was determined at 1.0 A resolution by single-wavelength anomalous diffraction. The fold is very similar to that of arsenate reductase, which is an extension of the thioredoxin fold. CONCLUSION: Given the conservation of the functionally important residues and the ability to bind glutathione, YffB is likely to function as a GSH-dependent thiol reductase.

About this StructureAbout this Structure

1RW1 is a Single protein structure of sequence from Pseudomonas aeruginosa pao1 with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the YffB protein from Pseudomonas aeruginosa suggests a glutathione-dependent thiol reductase function., Teplyakov A, Pullalarevu S, Obmolova G, Doseeva V, Galkin A, Herzberg O, Dauter M, Dauter Z, Gilliland GL, BMC Struct Biol. 2004 Mar 8;4:5. PMID:15102337

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