1lxa: Difference between revisions

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New page: left|200px<br /><applet load="1lxa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lxa, resolution 2.6Å" /> '''UDP N-ACETYLGLUCOSAMI...
 
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[[Image:1lxa.jpg|left|200px]]<br /><applet load="1lxa" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1lxa.jpg|left|200px]]<br /><applet load="1lxa" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1lxa, resolution 2.6&Aring;" />
caption="1lxa, resolution 2.6&Aring;" />
'''UDP N-ACETYLGLUCOSAMINE ACYLTRANSFERASE'''<br />
'''UDP N-ACETYLGLUCOSAMINE ACYLTRANSFERASE'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1LXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LXA OCA].  
1LXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LXA OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Roderick, S.L.]]
[[Category: Roderick, S L.]]
[[Category: acyltransferase]]
[[Category: acyltransferase]]
[[Category: lipid a biosynthesis]]
[[Category: lipid a biosynthesis]]
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[[Category: transferase]]
[[Category: transferase]]


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