1bob

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(New page: 200px<br /><applet load="1bob" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bob, resolution 2.3&Aring;" /> '''HISTONE ACETYLTRANSFE...)
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[[Image:1bob.jpg|left|200px]]<br /><applet load="1bob" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bob, resolution 2.3&Aring;" />
 
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'''HISTONE ACETYLTRANSFERASE HAT1 FROM SACCHAROMYCES CEREVISIAE IN COMPLEX WITH ACETYL COENZYME A'''<br />
 
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==Overview==
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==HISTONE ACETYLTRANSFERASE HAT1 FROM SACCHAROMYCES CEREVISIAE IN COMPLEX WITH ACETYL COENZYME A==
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We have solved the crystal structure of the yeast histone, acetyltransferase Hat1-acetyl coenzyme A (AcCoA) complex at 2.3 A, resolution. Hat1 has an elongated, curved structure, and the AcCoA, molecule is bound in a cleft on the concave surface of the protein, marking the active site of the enzyme. A channel of variable width and, depth that runs across the protein is probably the binding site for the, histone substrate. A model for histone H4 binding by Hat1 is discussed in, terms of possible sources of specific lysine recognition by the enzyme., The structure of Hat1 provides a model for the structures of the catalytic, domains of a protein superfamily that includes other histone, acetyltransferases such as Gcn5 and CBP.
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<StructureSection load='1bob' size='340' side='right'caption='[[1bob]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bob]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BOB FirstGlance]. <br>
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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]] 2.3&#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=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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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=1bob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bob OCA], [https://pdbe.org/1bob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bob RCSB], [https://www.ebi.ac.uk/pdbsum/1bob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bob ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HAT1_YEAST HAT1_YEAST] Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of free histone H4 in the cytoplasm. The complex is also found in the nucleus, however it is not certain that it modifies histone H4 when packaged in chromatin. Histone H4 'Lys-12' acetylation is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.<ref>PMID:7559580</ref> <ref>PMID:10982821</ref> <ref>PMID:12417736</ref> <ref>PMID:14761951</ref> <ref>PMID:15099519</ref>
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== Evolutionary Conservation ==
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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/bo/1bob_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=1bob ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1BOB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with CA and ACO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BOB OCA].
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*[[Histone acetyltransferase|Histone acetyltransferase]]
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*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
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==Reference==
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== References ==
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Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily., Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V, Cell. 1998 Aug 21;94(4):427-38. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9727486 9727486]
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<references/>
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[[Category: Histone acetyltransferase]]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Dutnall RN]]
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[[Category: Dutnall, R.N.]]
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[[Category: Ramakrishnan V]]
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[[Category: Ramakrishnan, V.]]
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[[Category: Sternglanz R]]
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[[Category: Sternglanz, R.]]
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[[Category: Tafrov ST]]
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[[Category: Tafrov, S.T.]]
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[[Category: ACO]]
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[[Category: CA]]
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[[Category: acetyl coenzyme a binding-protein]]
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[[Category: histone acetyltransferase]]
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[[Category: histone modification]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:47:24 2007''
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Current revision

HISTONE ACETYLTRANSFERASE HAT1 FROM SACCHAROMYCES CEREVISIAE IN COMPLEX WITH ACETYL COENZYME A

PDB ID 1bob

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