1muu: Difference between revisions

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[[Image:1muu.gif|left|200px]]
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{{STRUCTURE_1muu|  PDB=1muu  |  SCENE=  }}  
{{STRUCTURE_1muu|  PDB=1muu  |  SCENE=  }}  


'''2.0 A crystal structure of GDP-mannose dehydrogenase'''
===2.0 A crystal structure of GDP-mannose dehydrogenase===




==Overview==
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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.
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{{ABSTRACT_PUBMED_12705829}}


==About this Structure==
==About this Structure==
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[[Category: Enzyme complex with cofactor and product]]
[[Category: Enzyme complex with cofactor and product]]
[[Category: Rossman fold]]
[[Category: Rossman fold]]
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Revision as of 12:11, 28 July 2008

File:1muu.png

Template:STRUCTURE 1muu

2.0 A crystal structure of GDP-mannose dehydrogenase

Template:ABSTRACT PUBMED 12705829

About this Structure

1MUU 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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