2i2w

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[[Image:2i2w.jpg|left|200px]]
[[Image:2i2w.jpg|left|200px]]
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{{Structure
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|PDB= 2i2w |SIZE=350|CAPTION= <scene name='initialview01'>2i2w</scene>, resolution 1.95&Aring;
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The line below this paragraph, containing "STRUCTURE_2i2w", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Residue+D+196'>AC1</scene>
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|GENE= gmhA, lpcA, tfrA, b0222 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_2i2w| PDB=2i2w | SCENE= }}
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|RELATEDENTRY=[[2i22|2I22]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i2w OCA], [http://www.ebi.ac.uk/pdbsum/2i2w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i2w RCSB]</span>
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'''Crystal Structure of Escherichia Coli Phosphoheptose Isomerase'''
'''Crystal Structure of Escherichia Coli Phosphoheptose Isomerase'''
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[[Category: Wright, G.]]
[[Category: Wright, G.]]
[[Category: Zhang, K.]]
[[Category: Zhang, K.]]
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[[Category: lipopolysaccharide biosynthesis]]
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[[Category: Lipopolysaccharide biosynthesis]]
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[[Category: phosphoheptose isomerase]]
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[[Category: Phosphoheptose isomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:00:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:38:58 2008''
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Revision as of 04:00, 4 May 2008

Template:STRUCTURE 2i2w

Crystal Structure of Escherichia Coli 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

2I2W is a Single protein structure of sequence from Escherichia coli. 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 Sun May 4 07:00:29 2008

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