2vfb
From Proteopedia
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| - | [[Image:2vfb.jpg|left|200px]] | + | [[Image:2vfb.jpg|left|200px]] |
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| - | '''THE STRUCTURE OF MYCOBACTERIUM MARINUM ARYLAMINE N-ACETYLTRANSFERASE''' | + | {{Structure |
| + | |PDB= 2vfb |SIZE=350|CAPTION= <scene name='initialview01'>2vfb</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Arylamine_N-acetyltransferase Arylamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.5 2.3.1.5] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE STRUCTURE OF MYCOBACTERIUM MARINUM ARYLAMINE N-ACETYLTRANSFERASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2VFB is a [ | + | 2VFB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_marinum Mycobacterium marinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFB OCA]. |
==Reference== | ==Reference== | ||
| - | Divergence of cofactor recognition across evolution: coenzyme A binding in a prokaryotic arylamine N-acetyltransferase., Fullam E, Westwood IM, Anderton MC, Lowe ED, Sim E, Noble ME, J Mol Biol. 2008 Jan 4;375(1):178-91. Epub 2007 Oct 13. PMID:[http:// | + | Divergence of cofactor recognition across evolution: coenzyme A binding in a prokaryotic arylamine N-acetyltransferase., Fullam E, Westwood IM, Anderton MC, Lowe ED, Sim E, Noble ME, J Mol Biol. 2008 Jan 4;375(1):178-91. Epub 2007 Oct 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18005984 18005984] |
[[Category: Arylamine N-acetyltransferase]] | [[Category: Arylamine N-acetyltransferase]] | ||
[[Category: Mycobacterium marinum]] | [[Category: Mycobacterium marinum]] | ||
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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 18:45:56 2008'' |
Revision as of 16:45, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Activity: | Arylamine N-acetyltransferase, with EC number 2.3.1.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURE OF MYCOBACTERIUM MARINUM ARYLAMINE N-ACETYLTRANSFERASE
Overview
Arylamine N-acetyltransferase (NAT) enzymes are widespread in nature. They serve to acetylate xenobiotics and/or endogenous substrates using acetyl coenzyme A (CoA) as a cofactor. Conservation of the architecture of the NAT enzyme family from mammals to bacteria has been demonstrated by a series of prokaryotic NAT structures, together with the recently reported structure of human NAT1. We report here the cloning, purification, kinetic characterisation and crystallographic structure determination of NAT from Mycobacterium marinum, a close relative of the pathogenic Mycobacterium tuberculosis. We have also determined the structure of M. marinum NAT in complex with CoA, shedding the first light on cofactor recognition in prokaryotic NATs. Surprisingly, the principal CoA recognition site in M. marinum NAT is located some 30 A from the site of CoA recognition in the recently deposited structure of human NAT2 bound to CoA. The structure explains the Ping-Pong Bi-Bi reaction mechanism of NAT enzymes and suggests mechanisms by which the acetylated enzyme intermediate may be protected. Recognition of CoA in a much wider groove in prokaryotic NATs suggests that this subfamily may accommodate larger substrates than is the case for human NATs and may assist in the identification of potential endogenous substrates. It also suggests the cofactor-binding site as a unique subsite to target in drug design directed against NAT in mycobacteria.
About this Structure
2VFB is a Single protein structure of sequence from Mycobacterium marinum. Full crystallographic information is available from OCA.
Reference
Divergence of cofactor recognition across evolution: coenzyme A binding in a prokaryotic arylamine N-acetyltransferase., Fullam E, Westwood IM, Anderton MC, Lowe ED, Sim E, Noble ME, J Mol Biol. 2008 Jan 4;375(1):178-91. Epub 2007 Oct 13. PMID:18005984
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