1lxa

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{{STRUCTURE_1lxa| PDB=1lxa | SCENE= }}
{{STRUCTURE_1lxa| PDB=1lxa | SCENE= }}
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'''UDP N-ACETYLGLUCOSAMINE ACYLTRANSFERASE'''
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===UDP N-ACETYLGLUCOSAMINE ACYLTRANSFERASE===
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==Overview==
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UDP-N-acetylglucosamine 3-O-acyltransferase (LpxA) catalyzes the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-N-acetylglucosamine. LpxA is the first enzyme in the lipid A biosynthetic pathway and is a target for the design of antibiotics. The x-ray crystal structure of LpxA has been determined to 2.6 angstrom resolution and reveals a domain motif composed of parallel beta strands, termed a left-handed parallel beta helix (L beta H). This unusual fold displays repeated violations of the protein folding constraint requiring right-handed crossover connections between strands of parallel beta sheets and may be present in other enzymes that share amino acid sequence homology to the repeated hexapeptide motif of LpxA.
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(as it appears on PubMed at http://www.pubmed.gov), where 7481807 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7481807}}
==About this Structure==
==About this Structure==
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[[Category: Lipid synthesis]]
[[Category: Lipid synthesis]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:45:13 2008''

Revision as of 19:45, 2 July 2008

Template:STRUCTURE 1lxa

UDP N-ACETYLGLUCOSAMINE ACYLTRANSFERASE

Template:ABSTRACT PUBMED 7481807

About this Structure

1LXA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase., Raetz CR, Roderick SL, Science. 1995 Nov 10;270(5238):997-1000. PMID:7481807

Page seeded by OCA on Wed Jul 2 22:45:13 2008

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