1qsm

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[[Image:1qsm.gif|left|200px]]<br /><applet load="1qsm" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qsm, resolution 2.40&Aring;" />
 
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'''HISTONE ACETYLTRANSFERASE HPA2 FROM SACCHAROMYCES CEREVISIAE IN COMPLEX WITH ACETYL COENZYME A'''<br />
 
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==Overview==
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==Histone Acetyltransferase HPA2 from Saccharomyces Cerevisiae in Complex with Acetyl Coenzyme A==
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We report the crystal structure of the yeast protein Hpa2 in complex with acetyl coenzyme A (AcCoA) at 2.4 A resolution and without cofactor at 2.9 A resolution. Hpa2 is a member of the Gcn5-related N-acetyltransferase (GNAT) superfamily, a family of enzymes with diverse substrates including histones, other proteins, arylalkylamines and aminoglycosides. In vitro, Hpa2 is able to acetylate specific lysine residues of histones H3 and H4 with a preference for Lys14 of histone H3. Hpa2 forms a stable dimer in solution and forms a tetramer upon binding AcCoA. The crystal structure reveals that the Hpa2 tetramer is stabilized by base-pair interactions between the adenine moieties of the bound AcCoA molecules. These base-pairs represent a novel method of stabilizing an oligomeric protein structure. Comparison of the structure of Hpa2 with those of other GNAT superfamily members illustrates a remarkably conserved fold of the catalytic domain of the GNAT family even though members of this family share low levels of sequence homology. This comparison has allowed us to better define the borders of the four sequence motifs that characterize the GNAT family, including a motif that is not discernable in histone acetyltransferases by sequence comparison alone. We discuss implications of the Hpa2 structure for the catalytic mechanism of the GNAT enzymes and the opportunity for multiple histone tail modification created by the tetrameric Hpa2 structure.
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<StructureSection load='1qsm' size='340' side='right'caption='[[1qsm]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qsm]] is a 4 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=1QSM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QSM 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]] 2.4&#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></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=1qsm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qsm OCA], [https://pdbe.org/1qsm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qsm RCSB], [https://www.ebi.ac.uk/pdbsum/1qsm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qsm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HPA2_YEAST HPA2_YEAST] In vitro, acetylates histone H3 'Lys-4' and 'Lys-14' and histone H4 'Lys-5' and 'Lys-12'.
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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/qs/1qsm_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=1qsm 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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1QSM 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 <scene name='pdbligand=ACO:'>ACO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1QSM OCA].
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*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of the histone acetyltransferase Hpa2: A tetrameric member of the Gcn5-related N-acetyltransferase superfamily., Angus-Hill ML, Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V, J Mol Biol. 1999 Dec 17;294(5):1311-25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10600387 10600387]
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[[Category: Large Structures]]
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[[Category: Histone acetyltransferase]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Angus-Hill ML]]
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[[Category: Angus-Hill, M L.]]
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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: acetyltransferase]]
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[[Category: protein-acetyl coenzyme a complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:14 2008''
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Current revision

Histone Acetyltransferase HPA2 from Saccharomyces Cerevisiae in Complex with Acetyl Coenzyme A

PDB ID 1qsm

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