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2il4

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[[Image:2il4.gif|left|200px]]
 
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==Crystal structure of At1g77540-Coenzyme A Complex==
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The line below this paragraph, containing "STRUCTURE_2il4", creates the "Structure Box" on the page.
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<StructureSection load='2il4' size='340' side='right'caption='[[2il4]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.054&#8491;</td></tr>
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<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>
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{{STRUCTURE_2il4| PDB=2il4 | SCENE= }}
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<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>
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</table>
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'''Crystal structure of At1g77540-Coenzyme A Complex'''
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== Function ==
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[https://www.uniprot.org/uniprot/Y1754_ARATH Y1754_ARATH] Possesses in vitro histone acetyltransferase activity with histones H3 and H4.<ref>PMID:17128971</ref>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/2il4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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.
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==About this Structure==
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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>
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2IL4 is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17128971 17128971]
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</div>
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<div class="pdbe-citations 2il4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bingman, C A.]]
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[[Category: Bingman CA]]
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[[Category: Bitto, E.]]
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[[Category: Bitto E]]
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[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
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[[Category: Phillips Jr GN]]
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[[Category: Jr., G N.Phillips.]]
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[[Category: Wesenberg GE]]
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[[Category: Wesenberg, G E.]]
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[[Category: Acetyltransferase]]
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[[Category: At1g77540]]
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[[Category: Center for eukaryotic structural genomic]]
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[[Category: Cesg]]
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[[Category: Coa]]
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[[Category: Coenzyme-a]]
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[[Category: Cog2388 family]]
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[[Category: Protein structure initiative]]
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[[Category: Psi]]
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[[Category: Structural genomics functional follow-up study]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:37:12 2008''
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Current revision

Crystal structure of At1g77540-Coenzyme A Complex

PDB ID 2il4

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