4psx: Difference between revisions

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 <StructureSection load='4psx' size='340' side='right'caption='[[4psx]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4psx]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PSX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PSX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4psx]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PSX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.509&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HAT1, LPA16W, YP8132.12, YPL001W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), HAT2, YEL056W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), HHF1, YBR009C, YBR0122, HHF2, YNL030W, N2752 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=4psx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4psx OCA], [https://pdbe.org/4psx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4psx RCSB], [https://www.ebi.ac.uk/pdbsum/4psx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4psx ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4psx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4psx OCA], [http://pdbe.org/4psx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4psx RCSB], [http://www.ebi.ac.uk/pdbsum/4psx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4psx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>  [[http://www.uniprot.org/uniprot/HAT2_YEAST HAT2_YEAST]] Regulatory subunit of the histone acetylase B (HAT-B) complex. The complex acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. HAT2 is required for high affinity binding of the acetyltransferase to histone H4, for the nuclear location of HAT1 and for the HAT1-HIF1 interaction. Alone, it is unable to bind to H4, requiring HAT1 for high affinity interaction with the histone tail. HAT2 has also a HAT1 independent function in life-span regulation.<ref>PMID:10982821</ref> <ref>PMID:14761951</ref> <ref>PMID:15099519</ref> <ref>PMID:16023114</ref>
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 ==See Also==
-*[[Histone acetyltransferase|Histone acetyltransferase]]
+*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Baker's yeast]]
-[[Category: Histone acetyltransferase]]
 [[Category: Large Structures]]
-[[Category: Li, Y]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Yang, M]]
+[[Category: Li Y]]
-[[Category: Accoa]]
+[[Category: Yang M]]
-[[Category: Acetyltransferase]]
-[[Category: Hat wd40]]
-[[Category: Histone-transferase complex]]
-[[Category: Phosphorylation]]