1mv8
From Proteopedia
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|PDB= 1mv8 |SIZE=350|CAPTION= <scene name='initialview01'>1mv8</scene>, resolution 1.550Å | |PDB= 1mv8 |SIZE=350|CAPTION= <scene name='initialview01'>1mv8</scene>, resolution 1.550Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=GDX:GUANOSINE+5 | + | |LIGAND= <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=GDX:GUANOSINE+5'-(TRIHYDROGEN+DIPHOSPHATE),+P'-D-MANNOPYRANOSYL+ESTER'>GDX</scene>, <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> |
|ACTIVITY= [http://en.wikipedia.org/wiki/GDP-mannose_6-dehydrogenase GDP-mannose 6-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.132 1.1.1.132] | |ACTIVITY= [http://en.wikipedia.org/wiki/GDP-mannose_6-dehydrogenase GDP-mannose 6-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.132 1.1.1.132] | ||
|GENE= AlgD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa]) | |GENE= AlgD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa]) | ||
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[[Category: rossman fold]] | [[Category: rossman fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:48:59 2008'' |
Revision as of 10:49, 23 March 2008
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| , resolution 1.550Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , and | ||||||
| Gene: | AlgD (Pseudomonas aeruginosa) | ||||||
| Activity: | GDP-mannose 6-dehydrogenase, with EC number 1.1.1.132 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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