1rw1: Difference between revisions
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=" | [[Image:1rw1.gif|left|200px]]<br /><applet load="1rw1" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1rw1, resolution 1.02Å" /> | caption="1rw1, resolution 1.02Å" /> | ||
'''YFFB (PA3664) PROTEIN'''<br /> | '''YFFB (PA3664) PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
BACKGROUND: The yffB (PA3664) gene of Pseudomonas aeruginosa encodes an | 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:// | 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 | [[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 | [[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:// | ''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
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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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