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1rpn

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{{STRUCTURE_1rpn| PDB=1rpn | SCENE= }}
{{STRUCTURE_1rpn| PDB=1rpn | SCENE= }}
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'''Crystal Structure of GDP-D-mannose 4,6-dehydratase in complexes with GDP and NADPH'''
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===Crystal Structure of GDP-D-mannose 4,6-dehydratase in complexes with GDP and NADPH===
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==Overview==
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d-Rhamnose is a rare 6-deoxy monosaccharide primarily found in the lipopolysaccharide of pathogenic bacteria, where it is involved in host-bacterium interactions and the establishment of infection. The biosynthesis of d-rhamnose proceeds through the conversion of GDP-d-mannose by GDP-d-mannose 4,6-dehydratase (GMD) to GDP-4-keto-6-deoxymannose, which is subsequently reduced to GDP-d-rhamnose by a reductase. We have determined the crystal structure of GMD from Pseudomonas aeruginosa in complex with NADPH and GDP. GMD belongs to the NDP-sugar modifying subfamily of the short-chain dehydrogenase/reductase (SDR) enzymes, all of which exhibit bidomain structures and a conserved catalytic triad (Tyr-XXX-Lys and Ser/Thr). Although most members of this enzyme subfamily display homodimeric structures, this bacterial GMD forms a tetramer in the same fashion as the plant MUR1 from Arabidopsis thaliana. The cofactor binding sites are adjoined across the tetramer interface, which brings the adenosyl phosphate moieties of the adjacent NADPH molecules to within 7 A of each other. A short peptide segment (Arg35-Arg43) stretches into the neighboring monomer, making not only protein-protein interactions but also hydrogen bonding interactions with the neighboring cofactor. The interface hydrogen bonds made by the Arg35-Arg43 segment are generally conserved in GMD and MUR1, and the interacting residues are highly conserved among the sequences of bacterial and eukaryotic GMDs. Outside of the Arg35-Arg43 segment, residues involved in tetrameric contacts are also quite conserved across different species. These observations suggest that a tetramer is the preferred, and perhaps functionally relevant, oligomeric state for most bacterial and eukaryotic GMDs.
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(as it appears on PubMed at http://www.pubmed.gov), where 14739333 is the PubMed ID number.
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==About this Structure==
==About this Structure==
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[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
[[Category: Short-chain dehydrogenase/reductase]]
[[Category: Short-chain dehydrogenase/reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:45:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:53:17 2008''

Revision as of 10:53, 28 July 2008

Image:1rpn.png

Template:STRUCTURE 1rpn

Crystal Structure of GDP-D-mannose 4,6-dehydratase in complexes with GDP and NADPH

Template:ABSTRACT PUBMED 14739333

About this Structure

1RPN is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

Crystal structure of a tetrameric GDP-D-mannose 4,6-dehydratase from a bacterial GDP-D-rhamnose biosynthetic pathway., Webb NA, Mulichak AM, Lam JS, Rocchetta HL, Garavito RM, Protein Sci. 2004 Feb;13(2):529-39. PMID:14739333

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