1xmt

<table><tr><td colspan='2'>[[1xmt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XMT FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At1g77540 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmt OCA], [http://pdbe.org/1xmt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xmt RCSB], [http://www.ebi.ac.uk/pdbsum/1xmt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xmt ProSAT]</span></td></tr>

[[http://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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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1xmt" style="background-color:#fffaf0;"></div>

[[Category: Arath]]

[[Category: Allard, S T.M]]

[[Category: Bingman, C A]]

[[Category: Bitto, E]]

[[Category: Structural genomic]]

[[Category: Phillips, G N]]

[[Category: Smith, D W]]

[[Category: Wesenberg, G E]]

[[Category: Unknown function]]