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| {{STRUCTURE_2i2w| PDB=2i2w | SCENE= }} | | {{STRUCTURE_2i2w| PDB=2i2w | SCENE= }} |
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| '''Crystal Structure of Escherichia Coli Phosphoheptose Isomerase'''
| | ===Crystal Structure of Escherichia Coli Phosphoheptose Isomerase=== |
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| ==Overview==
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| The barrier imposed by lipopolysaccharide (LPS) in the outer membrane of Gram-negative bacteria presents a significant challenge in treatment of these organisms with otherwise effective hydrophobic antibiotics. The absence of l-glycero-d-manno-heptose in the LPS molecule is associated with a dramatically increased bacterial susceptibility to hydrophobic antibiotics and thus enzymes in the ADP-heptose biosynthesis pathway are of significant interest. GmhA catalyzes the isomerization of d-sedoheptulose 7-phosphate into d-glycero-d-manno-heptose 7-phosphate, the first committed step in the formation of ADP-heptose. Here we report structures of GmhA from Escherichia coli and Pseudomonas aeruginosa in apo, substrate, and product-bound forms, which together suggest that GmhA adopts two distinct conformations during isomerization through reorganization of quaternary structure. Biochemical characterization of GmhA mutants, combined with in vivo analysis of LPS biosynthesis and novobiocin susceptibility, identifies key catalytic residues. We postulate GmhA acts through an enediol-intermediate isomerase mechanism. | | The line below this paragraph, {{ABSTRACT_PUBMED_18056714}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18056714 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18056714}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Lipopolysaccharide biosynthesis]] | | [[Category: Lipopolysaccharide biosynthesis]] |
| [[Category: Phosphoheptose isomerase]] | | [[Category: Phosphoheptose isomerase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:00:29 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:49:54 2008'' |
