4mxe

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==Human establishment factor-like protein 1==
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==Human ESCO1 (Eco1/Ctf7 ortholog), acetyltransferase domain in complex with acetyl-CoA==
<StructureSection load='4mxe' size='340' side='right' caption='[[4mxe]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='4mxe' size='340' side='right' caption='[[4mxe]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4mxe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MXE FirstGlance]. <br>
<table><tr><td colspan='2'>[[4mxe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MXE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mxe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mxe RCSB], [http://www.ebi.ac.uk/pdbsum/4mxe PDBsum]</span></td></tr>
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<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=4mxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mxe OCA], [http://pdbe.org/4mxe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mxe RCSB], [http://www.ebi.ac.uk/pdbsum/4mxe PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ESCO1_HUMAN ESCO1_HUMAN]] Acetyltransferase required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase. Acts by mediating the acetylation of cohesin component SMC3.<ref>PMID:14576321</ref> <ref>PMID:15958495</ref> <ref>PMID:18614053</ref> <ref>PMID:19907496</ref>
[[http://www.uniprot.org/uniprot/ESCO1_HUMAN ESCO1_HUMAN]] Acetyltransferase required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase. Acts by mediating the acetylation of cohesin component SMC3.<ref>PMID:14576321</ref> <ref>PMID:15958495</ref> <ref>PMID:18614053</ref> <ref>PMID:19907496</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Sister chromatid cohesion, formed by the cohesin protein complex, is essential for chromosome segregation. In order for cohesion to be established, the cohesin subunit SMC3 needs to be acetylated by a homolog of the ESCO1/Eco1 acetyltransferases, the enzymatic mechanism of which has remained unknown. Here we report the crystal structure of the ESCO1 acetyltransferase domain in complex with acetyl-coenzyme A, and show by SAXS that ESCO1 is a dimer in solution. The structure reveals an active site that lacks a potential catalytic base side chain. However, mutation of glutamate 789, a surface residue that is close to the automodification target lysine 803, strongly reduces autoacetylation of ESCO1. Moreover, budding yeast Smc3 mutated at the conserved residue D114, adjacent to the cohesion-activating acetylation site K112,K113, cannot be acetylated in vivo. This indicates that ESCO1 controls cohesion through substrate-assisted catalysis. Thus, this study discloses a key mechanism for cohesion establishment.
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Sister Chromatid Cohesion Establishment Factor ESCO1 Operates by Substrate-Assisted Catalysis.,Kouznetsova E, Kanno T, Karlberg T, Thorsell AG, Wisniewska M, Kursula P, Sjogren C, Schuler H Structure. 2016 May 3;24(5):789-96. doi: 10.1016/j.str.2016.03.021. Epub 2016 Apr, 21. PMID:27112597<ref>PMID:27112597</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4mxe" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 19:09, 10 May 2016

Human ESCO1 (Eco1/Ctf7 ortholog), acetyltransferase domain in complex with acetyl-CoA

4mxe, resolution 2.60Å

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