2il4
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:2il4.png|left|200px]] | ||
- | < | + | ==Crystal structure of At1g77540-Coenzyme A Complex== |
- | + | <StructureSection load='2il4' size='340' side='right'caption='[[2il4]], [[Resolution|resolution]] 2.05Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[2il4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2gdb 2gdb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IL4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IL4 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]] 2.054Å</td></tr> | |
- | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</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=2il4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2il4 OCA], [https://pdbe.org/2il4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2il4 RCSB], [https://www.ebi.ac.uk/pdbsum/2il4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2il4 ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Y1754_ARATH Y1754_ARATH] Possesses in vitro histone acetyltransferase activity with histones H3 and H4.<ref>PMID:17128971</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/il/2il4_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2il4 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | We describe X-ray crystal and NMR solution structures of the protein coded for by Arabidopsis thaliana gene At1g77540.1 (At1g77540). The crystal structure was determined to 1.15 A with an R factor of 14.9% (Rfree = 17.0%) by multiple-wavelength anomalous diffraction using sodium bromide derivatized crystals. The ensemble of NMR conformers was determined with protein samples labeled with 15N and 13C + 15N. The X-ray structure and NMR ensemble were closely similar with rmsd 1.4 A for residues 8-93. At1g77540 was found to adopt a fold similar to that of GCN5-related N-acetyltransferases. Enzymatic activity assays established that At1g77540 possesses weak acetyltransferase activity against histones H3 and H4. Chemical shift perturbations observed in 15N-HSQC spectra upon the addition of CoA indicated that the cofactor binds and identified its binding site. The molecular details of this interaction were further elucidated by solving the X-ray structure of the At1g77540-CoA complex. This work establishes that the domain family COG2388 represents a novel class of acetyltransferase and provides insight into possible mechanistic roles of the conserved Cys76 and His41 residues of this family. | ||
- | + | Structure of Arabidopsis thaliana At1g77540 protein, a minimal acetyltransferase from the COG2388 family.,Tyler RC, Bitto E, Berndsen CE, Bingman CA, Singh S, Lee MS, Wesenberg GE, Denu JM, Phillips GN Jr, Markley JL Biochemistry. 2006 Dec 5;45(48):14325-36. PMID:17128971<ref>PMID:17128971</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 2il4" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | |
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[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Bingman | + | [[Category: Bingman CA]] |
- | [[Category: Bitto | + | [[Category: Bitto E]] |
- | + | [[Category: Phillips Jr GN]] | |
- | [[Category: Jr | + | [[Category: Wesenberg GE]] |
- | [[Category: Wesenberg | + | |
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Current revision
Crystal structure of At1g77540-Coenzyme A Complex
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