1k35
From Proteopedia
(New page: 200px<br /><applet load="1k35" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k35, resolution 2.2Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1k35.gif|left|200px]]<br /><applet load="1k35" size=" | + | [[Image:1k35.gif|left|200px]]<br /><applet load="1k35" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k35, resolution 2.2Å" /> | caption="1k35, resolution 2.2Å" /> | ||
'''Crystal Structure of Phosphomannomutase/Phosphoglucomutase from P.aeruginosa'''<br /> | '''Crystal Structure of Phosphomannomutase/Phosphoglucomutase from P.aeruginosa'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from P. | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1K35 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphomannomutase Phosphomannomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.8 5.4.2.8] Full crystallographic information is available from [http:// | + | 1K35 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphomannomutase Phosphomannomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.8 5.4.2.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K35 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Beamer, L | + | [[Category: Beamer, L J.]] |
[[Category: Regni, C.]] | [[Category: Regni, C.]] | ||
| - | [[Category: Tipton, P | + | [[Category: Tipton, P A.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: alpha/beta protein]] | [[Category: alpha/beta protein]] | ||
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[[Category: phosphoserine]] | [[Category: phosphoserine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:34 2008'' |
Revision as of 11:29, 21 February 2008
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Crystal Structure of Phosphomannomutase/Phosphoglucomutase from P.aeruginosa
Overview
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.
About this Structure
1K35 is a Single protein structure of sequence from Pseudomonas aeruginosa with as ligand. Active as Phosphomannomutase, with EC number 5.4.2.8 Full crystallographic information is available from OCA.
Reference
Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors., Regni C, Tipton PA, Beamer LJ, Structure. 2002 Feb;10(2):269-79. PMID:11839312
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