1xat: Difference between revisions
New page: left|200px<br /><applet load="1xat" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xat, resolution 3.20Å" /> '''STRUCTURE OF THE HEX... |
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[[Image:1xat.jpg|left|200px]]<br /><applet load="1xat" size=" | [[Image:1xat.jpg|left|200px]]<br /><applet load="1xat" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1xat, resolution 3.20Å" /> | caption="1xat, resolution 3.20Å" /> | ||
'''STRUCTURE OF THE HEXAPEPTIDE XENOBIOTIC ACETYLTRANSFERASE FROM PSEUDOMONAS AERUGINOSA'''<br /> | '''STRUCTURE OF THE HEXAPEPTIDE XENOBIOTIC ACETYLTRANSFERASE FROM PSEUDOMONAS AERUGINOSA'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of the xenobiotic acetyltransferase from Pseudomonas | The crystal structure of the xenobiotic acetyltransferase from Pseudomonas aeruginosa PA103 (PaXAT) has been determined, as well as that of its complex with the substrate chloramphenicol and the cofactor analogue desulfo-coenzyme A. PaXAT is a member of the large hexapeptide acyltransferase family of enzymes that display tandem repeated copies of a six-residue hexapeptide repeat sequence motif encoding a left-handed parallel beta helix (L betaH) structural domain. The xenobiotic acetyltransferase class of hexapeptide acyltransferases is composed of microbial enzymes that utilize acetyl-CoA to acylate a variety of hydroxyl-bearing acceptors. The active site of trimeric PaXAT is a short tunnel into which chloramphenicol and the cofactor analogue desulfo-CoA project from opposite ends. This tunnel is formed by the flat parallel beta sheets of two separate L betaH domains and an extended 39-residue loop. His 79 of the extended loop forms hydrogen bonds from its imidazole NE2 atom to the 3-hydroxyl group of chloramphenicol and from its ND1 group to the peptide oxygen of Thr 86. The interactions of this histidine residue are similar to those found in the structurally unrelated type III chloramphenicol acetyltransferase and suggest that His 79 of PaXAT may be similarly positioned and tautomerically stabilized to serve as a general base catalyst. | ||
==About this Structure== | ==About this Structure== | ||
1XAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http:// | 1XAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XAT OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Beaman, T | [[Category: Beaman, T W.]] | ||
[[Category: Roderick, S | [[Category: Roderick, S L.]] | ||
[[Category: Sugantino, M.]] | [[Category: Sugantino, M.]] | ||
[[Category: acetyltransferase]] | [[Category: acetyltransferase]] | ||
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[[Category: xenobiotic]] | [[Category: xenobiotic]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:56 2008'' | ||
Revision as of 16:52, 21 February 2008
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STRUCTURE OF THE HEXAPEPTIDE XENOBIOTIC ACETYLTRANSFERASE FROM PSEUDOMONAS AERUGINOSA
OverviewOverview
The crystal structure of the xenobiotic acetyltransferase from Pseudomonas aeruginosa PA103 (PaXAT) has been determined, as well as that of its complex with the substrate chloramphenicol and the cofactor analogue desulfo-coenzyme A. PaXAT is a member of the large hexapeptide acyltransferase family of enzymes that display tandem repeated copies of a six-residue hexapeptide repeat sequence motif encoding a left-handed parallel beta helix (L betaH) structural domain. The xenobiotic acetyltransferase class of hexapeptide acyltransferases is composed of microbial enzymes that utilize acetyl-CoA to acylate a variety of hydroxyl-bearing acceptors. The active site of trimeric PaXAT is a short tunnel into which chloramphenicol and the cofactor analogue desulfo-CoA project from opposite ends. This tunnel is formed by the flat parallel beta sheets of two separate L betaH domains and an extended 39-residue loop. His 79 of the extended loop forms hydrogen bonds from its imidazole NE2 atom to the 3-hydroxyl group of chloramphenicol and from its ND1 group to the peptide oxygen of Thr 86. The interactions of this histidine residue are similar to those found in the structurally unrelated type III chloramphenicol acetyltransferase and suggest that His 79 of PaXAT may be similarly positioned and tautomerically stabilized to serve as a general base catalyst.
About this StructureAbout this Structure
1XAT is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the hexapeptide xenobiotic acetyltransferase from Pseudomonas aeruginosa., Beaman TW, Sugantino M, Roderick SL, Biochemistry. 1998 May 12;37(19):6689-96. PMID:9578552
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