1ghe

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{{STRUCTURE_1ghe| PDB=1ghe | SCENE= }}
{{STRUCTURE_1ghe| PDB=1ghe | SCENE= }}
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'''CRYSTAL STRUCTURE OF TABTOXIN RESISTANCE PROTEIN COMPLEXED WITH AN ACYL COENZYME A'''
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===CRYSTAL STRUCTURE OF TABTOXIN RESISTANCE PROTEIN COMPLEXED WITH AN ACYL COENZYME A===
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==Overview==
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Tabtoxin resistance protein (TTR) is an enzyme that renders tabtoxin-producing pathogens, such as Pseudomonas syringae, tolerant to their own phytotoxins. Here, we report the crystal structure of TTR complexed with its natural cofactor, acetyl coenzyme A (AcCoA), to 1.55A resolution. The binary complex forms a characteristic "V" shape for substrate binding and contains the four motifs conserved in the GCN5-related N-acetyltransferase (GNAT) superfamily, which also includes the histone acetyltransferases (HATs). A single-step mechanism is proposed to explain the function of three conserved residues, Glu92, Asp130 and Tyr141, in catalyzing the acetyl group transfer to its substrate. We also report that TTR possesses HAT activity and suggest an evolutionary relationship between TTR and other GNAT members.
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(as it appears on PubMed at http://www.pubmed.gov), where 12527305 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12527305}}
==About this Structure==
==About this Structure==
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[[Category: Zhao, N.]]
[[Category: Zhao, N.]]
[[Category: Acyl coenzyme a complex]]
[[Category: Acyl coenzyme a complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:33:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:17:21 2008''

Revision as of 02:17, 1 July 2008

Image:1ghe.png

Template:STRUCTURE 1ghe

CRYSTAL STRUCTURE OF TABTOXIN RESISTANCE PROTEIN COMPLEXED WITH AN ACYL COENZYME A

Template:ABSTRACT PUBMED 12527305

About this Structure

1GHE is a Single protein structure of sequence from Pseudomonas syringae pv. tabaci. Full crystallographic information is available from OCA.

Reference

Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation., He H, Ding Y, Bartlam M, Sun F, Le Y, Qin X, Tang H, Zhang R, Joachimiak A, Liu J, Zhao N, Rao Z, J Mol Biol. 2003 Jan 31;325(5):1019-30. PMID:12527305

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