3bjz
From Proteopedia
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| - | [[Image:3bjz.jpg|left|200px]] | + | [[Image:3bjz.jpg|left|200px]] |
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| - | '''Crystal structure of Pseudomonas aeruginosa phosphoheptose isomerase''' | + | {{Structure |
| + | |PDB= 3bjz |SIZE=350|CAPTION= <scene name='initialview01'>3bjz</scene>, resolution 2.40Å | ||
| + | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+198'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+B+198'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+C+198'>AC3</scene> and <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+D+198'>AC4</scene> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= gmhA, PA4425 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 Pseudomonas aeruginosa PAO1]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of Pseudomonas aeruginosa phosphoheptose isomerase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3BJZ is a [ | + | 3BJZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_pao1 Pseudomonas aeruginosa pao1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BJZ OCA]. |
==Reference== | ==Reference== | ||
| - | Structure and Function of Sedoheptulose-7-phosphate Isomerase, a Critical Enzyme for Lipopolysaccharide Biosynthesis and a Target for Antibiotic Adjuvants., Taylor PL, Blakely KM, de Leon GP, Walker JR, McArthur F, Evdokimova E, Zhang K, Valvano MA, Wright GD, Junop MS, J Biol Chem. 2008 Feb 1;283(5):2835-45. Epub 2007 Dec 3. PMID:[http:// | + | Structure and Function of Sedoheptulose-7-phosphate Isomerase, a Critical Enzyme for Lipopolysaccharide Biosynthesis and a Target for Antibiotic Adjuvants., Taylor PL, Blakely KM, de Leon GP, Walker JR, McArthur F, Evdokimova E, Zhang K, Valvano MA, Wright GD, Junop MS, J Biol Chem. 2008 Feb 1;283(5):2835-45. Epub 2007 Dec 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18056714 18056714] |
[[Category: Pseudomonas aeruginosa pao1]] | [[Category: Pseudomonas aeruginosa pao1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lipopolysaccharide biosynthesis]] | [[Category: lipopolysaccharide biosynthesis]] | ||
[[Category: mcsg]] | [[Category: mcsg]] | ||
| - | [[Category: midwest center for structural | + | [[Category: midwest center for structural genomic]] |
[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
[[Category: psi]] | [[Category: psi]] | ||
[[Category: sis domain]] | [[Category: sis domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:59:38 2008'' |
Revision as of 16:59, 20 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | and | ||||||
| Gene: | gmhA, PA4425 (Pseudomonas aeruginosa PAO1) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Pseudomonas aeruginosa phosphoheptose isomerase
Overview
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.
About this Structure
3BJZ is a Single protein structure of sequence from Pseudomonas aeruginosa pao1. Full crystallographic information is available from OCA.
Reference
Structure and Function of Sedoheptulose-7-phosphate Isomerase, a Critical Enzyme for Lipopolysaccharide Biosynthesis and a Target for Antibiotic Adjuvants., Taylor PL, Blakely KM, de Leon GP, Walker JR, McArthur F, Evdokimova E, Zhang K, Valvano MA, Wright GD, Junop MS, J Biol Chem. 2008 Feb 1;283(5):2835-45. Epub 2007 Dec 3. PMID:18056714
Page seeded by OCA on Thu Mar 20 18:59:38 2008
Categories: Pseudomonas aeruginosa pao1 | Single protein | Evdokimova, E. | Joachimiak, A. | Kudritska, M. | MCSG, Midwest Center for Structural Genomics. | Osipiuk, J. | Savchenko, A. | Walker, J R. | CL | SO4 | Alpha/beta protein | Carbohydrate metabolism | Cytoplasm | Isomerase | Lipopolysaccharide biosynthesis | Mcsg | Midwest center for structural genomic | Protein structure initiative | Psi | Sis domain
