1e2t
From Proteopedia
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| - | [[Image:1e2t.gif|left|200px]] | + | [[Image:1e2t.gif|left|200px]] |
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| - | '''ARYLAMINE N-ACETYLTRANSFERASE (NAT) FROM SALMONELLA TYPHIMURIUM''' | + | {{Structure |
| + | |PDB= 1e2t |SIZE=350|CAPTION= <scene name='initialview01'>1e2t</scene>, resolution 2.8Å | ||
| + | |SITE= <scene name='pdbsite=AS1:Chain+A+Catalytic+Triad+Active+Site+CYS+69+Forms+Thio-Es+...'>AS1</scene>, <scene name='pdbsite=AS2:Chain+B+Catalytic+Triad+Active+Site+CYS+69+Forms+Thio-Es+...'>AS2</scene>, <scene name='pdbsite=AS3:Chain+C+Catalytic+Triad+Active+Site+CYS+69+Forms+Thio-Es+...'>AS3</scene>, <scene name='pdbsite=AS4:Chain+D+Catalytic+Triad+Active+Site+CYS+69+Forms+Thio-Es+...'>AS4</scene>, <scene name='pdbsite=AS5:Chain+E+Catalytic+Triad+Active+Site+CYS+69+Forms+Thio-Es+...'>AS5</scene>, <scene name='pdbsite=AS6:Chain+F+Catalytic+Triad+Active+Site+CYS+69+Forms+Thio-Es+...'>AS6</scene>, <scene name='pdbsite=AS7:Chain+G+Catalytic+Triad+Active+Site+CYS+69+Forms+Thio-Es+...'>AS7</scene> and <scene name='pdbsite=AS8:Chain+H+Catalytic+Triad+Active+Site+CYS+69+Forms+Thio-Es+...'>AS8</scene> | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/N-hydroxyarylamine_O-acetyltransferase N-hydroxyarylamine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.118 2.3.1.118] | ||
| + | |GENE= NHOA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=602 Salmonella typhimurium]) | ||
| + | }} | ||
| + | |||
| + | '''ARYLAMINE N-ACETYLTRANSFERASE (NAT) FROM SALMONELLA TYPHIMURIUM''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E2T is a [ | + | 1E2T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E2T OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of arylamine N-acetyltransferase reveals a catalytic triad., Sinclair JC, Sandy J, Delgoda R, Sim E, Noble ME, Nat Struct Biol. 2000 Jul;7(7):560-4. PMID:[http:// | + | Structure of arylamine N-acetyltransferase reveals a catalytic triad., Sinclair JC, Sandy J, Delgoda R, Sim E, Noble ME, Nat Struct Biol. 2000 Jul;7(7):560-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10876241 10876241] |
[[Category: N-hydroxyarylamine O-acetyltransferase]] | [[Category: N-hydroxyarylamine O-acetyltransferase]] | ||
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
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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 10:48:36 2008'' |
Revision as of 08:48, 20 March 2008
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| , resolution 2.8Å | |||||||
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| Sites: | , , , , , , and | ||||||
| Gene: | NHOA (Salmonella typhimurium) | ||||||
| Activity: | N-hydroxyarylamine O-acetyltransferase, with EC number 2.3.1.118 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ARYLAMINE N-ACETYLTRANSFERASE (NAT) FROM SALMONELLA TYPHIMURIUM
Overview
Enzymes of the arylamine N-acetyltransferase (NAT) family are found in species ranging from Escherichia coli to humans. In humans they are known to be responsible for the acetylation of a number of arylamine and hydrazine drugs, and they are strongly linked to the carcinogenic potentiation of certain foreign substances. In prokaryotes their substrate specificities may vary and members of the gene family have been linked to pathways including amide synthesis during rifamycin production. Here we report the crystal structure at 2.8 A resolution of a representative member of this family from Salmonella typhimurium in the presence and absence of a covalently bound product analog. The structure reveals surprising mechanistic information including the presence of a Cys-His-Asp catalytic triad. The fold can be described in terms of three domains of roughly equal length with the second and third domains linked by an interdomain helix. The first two domains, a helical bundle and a beta-barrel, make up the catalytic triad using a structural motif identical to that of the cysteine protease superfamily.
About this Structure
1E2T is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
Structure of arylamine N-acetyltransferase reveals a catalytic triad., Sinclair JC, Sandy J, Delgoda R, Sim E, Noble ME, Nat Struct Biol. 2000 Jul;7(7):560-4. PMID:10876241
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