1mv8
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(New page: 200px<br /><applet load="1mv8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mv8, resolution 1.550Å" /> '''1.55 A crystal stru...)
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Revision as of 19:36, 20 November 2007
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1.55 A crystal structure of a ternary complex of GDP-mannose dehydrogenase from Psuedomonas aeruginosa
Overview
The enzyme GMD from Pseudomonas aeruginosa catalyzes the committed step in, the synthesis of the exopolysaccharide alginate. Alginate is a major, component of P. aeruginosa biofilms that protect the bacteria from the, host immune response and antibiotic therapy. The 1.55 A crystal structure, of GMD in ternary complex with its cofactor NAD(H) and product, GDP-mannuronic acid reveals that the enzyme forms a domain-swapped dimer, with two polypeptide chains contributing to each active site. The, extensive dimer interface provides multiple opportunities for intersubunit, communication. Comparison of the GMD structure with that of UDP-glucose, dehydrogenase reveals the structural basis of sugar binding specificity, that distinguishes these two related enzyme families. The high-resolution, structure of GMD provides detailed information on the active site of the, enzyme and a template for structure-based inhibitor design.
About this Structure
1MV8 is a Single protein structure of sequence from Pseudomonas aeruginosa with SUC, NAD, GDX, ACY and MPD as ligands. Active as GDP-mannose 6-dehydrogenase, with EC number 1.1.1.132 Full crystallographic information is available from OCA.
Reference
Crystal structure of GDP-mannose dehydrogenase: a key enzyme of alginate biosynthesis in P. aeruginosa., Snook CF, Tipton PA, Beamer LJ, Biochemistry. 2003 Apr 29;42(16):4658-68. PMID:12705829
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