1e2t
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Enzymes of the arylamine N-acetyltransferase (NAT) family are found in | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Delgoda, R.]] | [[Category: Delgoda, R.]] | ||
| - | [[Category: Noble, M | + | [[Category: Noble, M E.M.]] |
[[Category: Sandy, J.]] | [[Category: Sandy, J.]] | ||
[[Category: Sim, E.]] | [[Category: Sim, E.]] | ||
| - | [[Category: Sinclair, J | + | [[Category: Sinclair, J C.]] |
[[Category: acetyl coa dependent]] | [[Category: acetyl coa dependent]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:10 2008'' |
Revision as of 10:23, 21 February 2008
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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. Active as N-hydroxyarylamine O-acetyltransferase, with EC number 2.3.1.118 Known structural/functional Sites: , , , , , , and . 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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