3oa2
From Proteopedia
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{{STRUCTURE_3oa2| PDB=3oa2 | SCENE= }} | {{STRUCTURE_3oa2| PDB=3oa2 | SCENE= }} | ||
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===Crystal structure of the WlbA (WbpB) dehydrogenase from Pseudomonas aeruginosa in complex with NAD at 1.5 angstrom resolution=== | ===Crystal structure of the WlbA (WbpB) dehydrogenase from Pseudomonas aeruginosa in complex with NAD at 1.5 angstrom resolution=== | ||
| + | {{ABSTRACT_PUBMED_20690587}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/P72133_PSEAE P72133_PSEAE]] Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the NAD-dependent oxidation of UDP-N-acetylglucosaminuronic acid (UDP-D-GlcNAcA) to UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronic acid (UDP-3-oxo-D-GlcNAcA). Can not use UDP-GlcNAc or UDP-GalNAc as the nucleotide sugar substrate, and can use only poorly UDP-D-glucuronic acid (UDP-GlcA). Undergoes an NAD(+) recycling mechanism using 2-oxoglutarate as an oxidant.<ref>PMID:18621892</ref> <ref>PMID:19348502</ref> <ref>PMID:19282284</ref> <ref>PMID:20690587</ref> | |
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==About this Structure== | ==About this Structure== | ||
| - | + | [[3oa2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OA2 OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020690587</ref><references group="xtra"/><references/> |
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Holden, H M.]] | [[Category: Holden, H M.]] | ||
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[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Sugar biosynthesis]] | [[Category: Sugar biosynthesis]] | ||
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Revision as of 11:56, 24 April 2013
Contents |
Crystal structure of the WlbA (WbpB) dehydrogenase from Pseudomonas aeruginosa in complex with NAD at 1.5 angstrom resolution
Template:ABSTRACT PUBMED 20690587
Function
[P72133_PSEAE] Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the NAD-dependent oxidation of UDP-N-acetylglucosaminuronic acid (UDP-D-GlcNAcA) to UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronic acid (UDP-3-oxo-D-GlcNAcA). Can not use UDP-GlcNAc or UDP-GalNAc as the nucleotide sugar substrate, and can use only poorly UDP-D-glucuronic acid (UDP-GlcA). Undergoes an NAD(+) recycling mechanism using 2-oxoglutarate as an oxidant.[1] [2] [3] [4]
About this Structure
3oa2 is a 4 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
- Thoden JB, Holden HM. Structural and Functional Studies of WlbA: A Dehydrogenase Involved in the Biosynthesis of 2,3-Diacetamido-2,3-dideoxy-d-mannuronic Acid . Biochemistry. 2010 Aug 19. PMID:20690587 doi:10.1021/bi101103s
- ↑ Westman EL, Preston A, Field RA, Lam JS. Biosynthesis of a rare di-N-acetylated sugar in the lipopolysaccharides of both Pseudomonas aeruginosa and Bordetella pertussis occurs via an identical scheme despite different gene clusters. J Bacteriol. 2008 Sep;190(18):6060-9. doi: 10.1128/JB.00579-08. Epub 2008 Jul 11. PMID:18621892 doi:10.1128/JB.00579-08
- ↑ Larkin A, Imperiali B. Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1. Biochemistry. 2009 Jun 16;48(23):5446-55. doi: 10.1021/bi900186u. PMID:19348502 doi:10.1021/bi900186u
- ↑ Westman EL, McNally DJ, Charchoglyan A, Brewer D, Field RA, Lam JS. Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa. J Biol Chem. 2009 May 1;284(18):11854-62. doi: 10.1074/jbc.M808583200. Epub 2009 , Mar 12. PMID:19282284 doi:10.1074/jbc.M808583200
- ↑ Thoden JB, Holden HM. Structural and Functional Studies of WlbA: A Dehydrogenase Involved in the Biosynthesis of 2,3-Diacetamido-2,3-dideoxy-d-mannuronic Acid . Biochemistry. 2010 Aug 19. PMID:20690587 doi:10.1021/bi101103s
