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New page: left|200px<br /><applet load="1ghe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ghe, resolution 1.55Å" /> '''CRYSTAL STRUCTURE OF... |
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== | ==CRYSTAL STRUCTURE OF TABTOXIN RESISTANCE PROTEIN COMPLEXED WITH AN ACYL COENZYME A== | ||
Tabtoxin resistance protein (TTR) is an enzyme that renders | <StructureSection load='1ghe' size='340' side='right'caption='[[1ghe]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ghe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_amygdali_pv._tabaci Pseudomonas amygdali pv. tabaci]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GHE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ghe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghe OCA], [https://pdbe.org/1ghe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ghe RCSB], [https://www.ebi.ac.uk/pdbsum/1ghe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghe ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TTR_PSEAJ TTR_PSEAJ] Renders tabtoxin-producing pathogens tolerant to their own phytotoxins.<ref>PMID:12527305</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gh/1ghe_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ghe ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:12527305</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1ghe" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Bartlam | <references/> | ||
[[Category: Ding | __TOC__ | ||
[[Category: He | </StructureSection> | ||
[[Category: Joachimiak | [[Category: Large Structures]] | ||
[[Category: Le | [[Category: Pseudomonas amygdali pv. tabaci]] | ||
[[Category: Liu | [[Category: Bartlam M]] | ||
[[Category: Qin | [[Category: Ding Y]] | ||
[[Category: Rao | [[Category: He H]] | ||
[[Category: Sun | [[Category: Joachimiak A]] | ||
[[Category: Tang | [[Category: Le Y]] | ||
[[Category: Zhang | [[Category: Liu Y]] | ||
[[Category: Zhao | [[Category: Qin X]] | ||
[[Category: Rao Z]] | |||
[[Category: Sun F]] | |||
[[Category: Tang H]] | |||
[[Category: Zhang R]] | |||
[[Category: Zhao N]] | |||
Latest revision as of 11:27, 6 November 2024
CRYSTAL STRUCTURE OF TABTOXIN RESISTANCE PROTEIN COMPLEXED WITH AN ACYL COENZYME ACRYSTAL STRUCTURE OF TABTOXIN RESISTANCE PROTEIN COMPLEXED WITH AN ACYL COENZYME A
Structural highlights
FunctionTTR_PSEAJ Renders tabtoxin-producing pathogens tolerant to their own phytotoxins.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTabtoxin 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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