1j4j
From Proteopedia
(New page: 200px<br /><applet load="1j4j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j4j, resolution 2.55Å" /> '''Crystal Structure of...) |
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| - | [[Image:1j4j.jpg|left|200px]]<br /><applet load="1j4j" size=" | + | [[Image:1j4j.jpg|left|200px]]<br /><applet load="1j4j" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1j4j, resolution 2.55Å" /> | caption="1j4j, resolution 2.55Å" /> | ||
'''Crystal Structure of Tabtoxin Resistance Protein (form II) complexed with an Acyl Coenzyme A'''<br /> | '''Crystal Structure of Tabtoxin Resistance Protein (form II) complexed with an Acyl Coenzyme A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Tabtoxin resistance protein (TTR) is an enzyme that renders | + | 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== | ==About this Structure== | ||
| - | 1J4J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tabaci Pseudomonas syringae pv. tabaci] with ACO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1J4J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tabaci Pseudomonas syringae pv. tabaci] with <scene name='pdbligand=ACO:'>ACO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J4J OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:49 2008'' |
Revision as of 11:18, 21 February 2008
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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 with as ligand. 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 Thu Feb 21 13:18:49 2008
Categories: Pseudomonas syringae pv. tabaci | Single protein | Bartlam, M. | Cao, Z. | Ding, Y. | Duke, N. | He, H. | Jiang, F. | Joachimiak, A. | Liu, J. | Liu, Y. | Rao, Z. | Shao, Y. | Tang, H. | Zhang, R. | Zhao, N. | ACO | Transferase
