1j4j
From Proteopedia
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- | [[Image:1j4j.jpg|left|200px]] | ||
- | < | + | ==Crystal Structure of Tabtoxin Resistance Protein (form II) complexed with an Acyl Coenzyme A== |
- | + | <StructureSection load='1j4j' size='340' side='right'caption='[[1j4j]], [[Resolution|resolution]] 2.55Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[1j4j]] 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=1J4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J4J 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]] 2.55Å</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=1j4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j4j OCA], [https://pdbe.org/1j4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j4j RCSB], [https://www.ebi.ac.uk/pdbsum/1j4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j4j 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/j4/1j4j_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=1j4j 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. | 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 1j4j" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | == References == |
- | [[Category: Bartlam | + | <references/> |
- | [[Category: Cao | + | __TOC__ |
- | [[Category: Ding | + | </StructureSection> |
- | [[Category: Duke | + | [[Category: Large Structures]] |
- | [[Category: He | + | [[Category: Pseudomonas amygdali pv. tabaci]] |
- | [[Category: Jiang | + | [[Category: Bartlam M]] |
- | [[Category: Joachimiak | + | [[Category: Cao Z]] |
- | [[Category: Liu | + | [[Category: Ding Y]] |
- | [[Category: Liu | + | [[Category: Duke N]] |
- | [[Category: Rao | + | [[Category: He H]] |
- | [[Category: Shao | + | [[Category: Jiang F]] |
- | [[Category: Tang | + | [[Category: Joachimiak A]] |
- | [[Category: Zhang | + | [[Category: Liu J]] |
- | [[Category: Zhao | + | [[Category: Liu Y]] |
- | + | [[Category: Rao Z]] | |
- | + | [[Category: Shao Y]] | |
+ | [[Category: Tang H]] | ||
+ | [[Category: Zhang R]] | ||
+ | [[Category: Zhao N]] |
Current revision
Crystal Structure of Tabtoxin Resistance Protein (form II) complexed with an Acyl Coenzyme A
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Categories: Large Structures | Pseudomonas amygdali pv. tabaci | 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