1j4j

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j4j OCA], [http://www.ebi.ac.uk/pdbsum/1j4j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j4j RCSB]</span>
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'''Crystal Structure of Tabtoxin Resistance Protein (form II) complexed with an Acyl Coenzyme A'''
'''Crystal Structure of Tabtoxin Resistance Protein (form II) complexed with an Acyl Coenzyme A'''
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[[Category: Zhang, R.]]
[[Category: Zhang, R.]]
[[Category: Zhao, N.]]
[[Category: Zhao, N.]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:47:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:28:41 2008''
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Revision as of 17:47, 2 May 2008

Template:STRUCTURE 1j4j

Crystal Structure of Tabtoxin Resistance Protein (form II) complexed with an Acyl Coenzyme A


Overview

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.

About this Structure

1J4J 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 Page seeded by OCA on Fri May 2 20:47:40 2008

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