1lxa
From Proteopedia
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[[Image:1lxa.png|left|200px]] | [[Image:1lxa.png|left|200px]] | ||
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{{STRUCTURE_1lxa| PDB=1lxa | SCENE= }} | {{STRUCTURE_1lxa| PDB=1lxa | SCENE= }} | ||
===UDP N-ACETYLGLUCOSAMINE ACYLTRANSFERASE=== | ===UDP N-ACETYLGLUCOSAMINE ACYLTRANSFERASE=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1lxa]] is a 1 chain structure with 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=1LXA OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:007481807</ref><ref group="xtra">PMID:011880627</ref><ref group="xtra">PMID:019456129</ref><references group="xtra"/> |
| - | [[Category: Escherichia coli | + | [[Category: Escherichia coli]] |
[[Category: Roderick, S L.]] | [[Category: Roderick, S L.]] | ||
[[Category: Acyltransferase]] | [[Category: Acyltransferase]] | ||
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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 1 09:46:09 2009'' | ||
Revision as of 20:07, 5 December 2012
UDP N-ACETYLGLUCOSAMINE ACYLTRANSFERASE
Template:ABSTRACT PUBMED 7481807
About this Structure
1lxa is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Raetz CR, Roderick SL. A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science. 1995 Nov 10;270(5238):997-1000. PMID:7481807
- Richardson JS, Richardson DC. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2754-9. PMID:11880627 doi:10.1073/pnas.052706099
- Robins LI, Williams AH, Raetz CR. Structural basis for the sugar nucleotide and acyl-chain selectivity of Leptospira interrogans LpxA. Biochemistry. 2009 Jul 7;48(26):6191-201. PMID:19456129 doi:10.1021/bi900629e
