1qso: Difference between revisions

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-[[Image:1qso.gif|left|200px]]<br /><applet load="1qso" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1qso, resolution 2.90&Aring;" />
-'''HISTONE ACETYLTRANSFERASE HPA2 FROM SACCHAROMYCES CEREVISIAE'''<br />
-==Overview==
+==Histone Acetyltransferase HPA2 from Saccharomyces Cerevisiae==
-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.
+<StructureSection load='1qso' size='340' side='right'caption='[[1qso]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1qso]] 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=1QSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QSO 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]] 2.9&#8491;</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=1qso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qso OCA], [https://pdbe.org/1qso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qso RCSB], [https://www.ebi.ac.uk/pdbsum/1qso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qso ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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'.
+== 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/qs/1qso_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=1qso ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-QSO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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=1QSO OCA].
+*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-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]
+[[Category: Large Structures]]
-[[Category: Histone acetyltransferase]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Single protein]]
+[[Category: Angus-Hill ML]]
-[[Category: Angus-Hill, M.L.]]
+[[Category: Dutnall RN]]
-[[Category: Dutnall, R.N.]]
+[[Category: Ramakrishnan V]]
-[[Category: Ramakrishnan, V.]]
+[[Category: Sterngalnz R]]
-[[Category: Sterngalnz, R.]]
+[[Category: Tafrov ST]]
-[[Category: Tafrov, S.T.]]
-[[Category: histone acetyltransferase]]
-[[Category: tetramer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:56:59 2007''