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| [[Image:1k35.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1k35| PDB=1k35 | SCENE= }} | | {{STRUCTURE_1k35| PDB=1k35 | SCENE= }} |
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| '''Crystal Structure of Phosphomannomutase/Phosphoglucomutase from P.aeruginosa'''
| | ===Crystal Structure of Phosphomannomutase/Phosphoglucomutase from P.aeruginosa=== |
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| ==Overview==
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| The enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from P. aeruginosa is required for the biosynthesis of two bacterial exopolysaccharides: alginate and lipopolysaccharide (LPS). Both of these molecules play a role in the virulence of P. aeruginosa, an important human pathogen known for its ability to develop antibiotic resistance and cause chronic lung infections in cystic fibrosis patients. The crystal structure of PMM/PGM shows that the enzyme has four domains, three of which have a similar three-dimensional fold. Residues from all four domains of the protein contribute to the formation of a large active site cleft in the center of the molecule. Detailed information on the active site of PMM/PGM lays the foundation for structure-based inhibitor design. Inhibitors of sufficient potency and specificity should impair the biosynthesis of alginate and LPS, and may facilitate clearance of the bacteria by the host immune system and increase the efficacy of conventional antibiotic treatment against chronic P. aeruginosa infections. | | The line below this paragraph, {{ABSTRACT_PUBMED_11839312}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11839312 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11839312}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Enzyme-metal complex]] | | [[Category: Enzyme-metal complex]] |
| [[Category: Phosphoserine]] | | [[Category: Phosphoserine]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:14:32 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 22:34:22 2008'' |
