1qso: Difference between revisions

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<StructureSection load='1qso' size='340' side='right'caption='[[1qso]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='1qso' size='340' side='right'caption='[[1qso]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qso]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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>
<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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span></td></tr>
</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>
<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>
</table>
== Function ==
== 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'.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1qso ConSurf].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:10600387<ref>PMID:10600387</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1qso" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Histone acetyltransferase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Angus-Hill, M L]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Dutnall, R N]]
[[Category: Angus-Hill ML]]
[[Category: Ramakrishnan, V]]
[[Category: Dutnall RN]]
[[Category: Sterngalnz, R]]
[[Category: Ramakrishnan V]]
[[Category: Tafrov, S T]]
[[Category: Sterngalnz R]]
[[Category: Tetramer]]
[[Category: Tafrov ST]]
[[Category: Transferase]]

Latest revision as of 11:17, 14 February 2024

Histone Acetyltransferase HPA2 from Saccharomyces CerevisiaeHistone Acetyltransferase HPA2 from Saccharomyces Cerevisiae

Structural highlights

1qso is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HPA2_YEAST In vitro, acetylates histone H3 'Lys-4' and 'Lys-14' and histone H4 'Lys-5' and 'Lys-12'.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1qso, resolution 2.90Å

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OCA
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