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2qiv
From Proteopedia
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| - | [[Image:2qiv.jpg|left|200px]] | + | [[Image:2qiv.jpg|left|200px]] |
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| - | '''Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase''' | + | {{Structure |
| + | |PDB= 2qiv |SIZE=350|CAPTION= <scene name='initialview01'>2qiv</scene>, resolution 1.850Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=U21:uridine-5'-diphosphate-3-O-(R-3-hydroxydecanoyl)-N-acetyl-D-glucosamine'>U21</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine_O-acyltransferase Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.129 2.3.1.129] | ||
| + | |GENE= lpxa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2QIV is a [ | + | 2QIV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QIV OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase., Williams AH, Raetz CR, Proc Natl Acad Sci U S A. 2007 Aug 21;104(34):13543-50. Epub 2007 Aug 13. PMID:[http:// | + | Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase., Williams AH, Raetz CR, Proc Natl Acad Sci U S A. 2007 Aug 21;104(34):13543-50. Epub 2007 Aug 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17698807 17698807] |
[[Category: Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase]] | [[Category: Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''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 18:26:15 2008'' |
Revision as of 16:26, 20 March 2008
| |||||||
| , resolution 1.850Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | lpxa (Escherichia coli) | ||||||
| Activity: | [acyl-carrier-protein--UDP-N-acetylglucosamine_O-acyltransferase Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase], with EC number 2.3.1.129 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase
Overview
UDP-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes the first step of lipid A biosynthesis, the reversible transfer of the R-3-hydroxyacyl chain from R-3-hydroxyacyl acyl carrier protein to the glucosamine 3-OH group of UDP-GlcNAc. Escherichia coli LpxA is highly selective for R-3-hydroxymyristate. The crystal structure of the E. coli LpxA homotrimer, determined previously in the absence of lipid substrates or products, revealed that LpxA contains an unusual, left-handed parallel beta-helix fold. We have now solved the crystal structures of E. coli LpxA with the bound product UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc at a resolution of 1.74 A and with bound UDP-3-O-(R-3-hydroxydecanoyl)-GlcNAc at 1.85 A. The structures of these complexes are consistent with the catalytic mechanism deduced by mutagenesis and with a recent 3.0-A structure of LpxA with bound UDP-GlcNAc. Our structures show how LpxA selects for 14-carbon R-3-hydroxyacyl chains and reveal two modes of UDP binding.
About this Structure
2QIV is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase., Williams AH, Raetz CR, Proc Natl Acad Sci U S A. 2007 Aug 21;104(34):13543-50. Epub 2007 Aug 13. PMID:17698807 [[Category: Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase]]
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