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4pw5

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<StructureSection load='4pw5' size='340' side='right' caption='[[4pw5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='4pw5' size='340' side='right' caption='[[4pw5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4pw5]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PW5 OCA]. <br>
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<table><tr><td colspan='2'>[[4pw5]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PW5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PW5 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5HC:2-DEOXY-5-(HYDROXYMETHYL)CYTIDINE+5-(DIHYDROGEN+PHOSPHATE)'>5HC</scene></td></tr>
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5HC:2-DEOXY-5-(HYDROXYMETHYL)CYTIDINE+5-(DIHYDROGEN+PHOSPHATE)'>5HC</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pw6|4pw6]], [[4pw7|4pw7]]</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pw6|4pw6]], [[4pw7|4pw7]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
 
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pw5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pw5 RCSB], [http://www.ebi.ac.uk/pdbsum/4pw5 PDBsum]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pw5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pw5 RCSB], [http://www.ebi.ac.uk/pdbsum/4pw5 PDBsum]</span></td></tr>
<table>
<table>
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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/UHRF2_HUMAN UHRF2_HUMAN]] E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131.<ref>PMID:12176013</ref> <ref>PMID:15178429</ref> <ref>PMID:14741369</ref> <ref>PMID:15361834</ref> <ref>PMID:21952639</ref> <ref>PMID:23404503</ref>
[[http://www.uniprot.org/uniprot/UHRF2_HUMAN UHRF2_HUMAN]] E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131.<ref>PMID:12176013</ref> <ref>PMID:15178429</ref> <ref>PMID:14741369</ref> <ref>PMID:15361834</ref> <ref>PMID:21952639</ref> <ref>PMID:23404503</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Methylated cytosine of CpG dinucleotides in vertebrates may be oxidized by Tet proteins, a process that can lead to DNA demethylation. The predominant oxidation product, 5-hydroxymethylcytosine (5hmC), has been implicated in embryogenesis, cell differentiation, and human diseases. Recently, the SRA domain of UHRF2 (UHRF2-SRA) has been reported to specifically recognize 5hmC, but how UHRF2 recognizes this modification is unclear. Here we report the structure of UHRF2-SRA in complex with a 5hmC-containing DNA. The structure reveals that the conformation of a phenylalanine allows the formation of an optimal 5hmC binding pocket, and a hydrogen bond between the hydroxyl group of 5hmC and UHRF2-SRA is critical for their preferential binding. Further structural and biochemical analyses unveiled the role of SRA domains as a versatile reader of modified DNA, and the knowledge should facilitate further understanding of the biological function of UHRF2 and the comprehension of DNA hydroxymethylation in general.
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Structural Basis for Hydroxymethylcytosine Recognition by the SRA Domain of UHRF2.,Zhou T, Xiong J, Wang M, Yang N, Wong J, Zhu B, Xu RM Mol Cell. 2014 May 7. pii: S1097-2765(14)00313-X. doi:, 10.1016/j.molcel.2014.04.003. PMID:24813944<ref>PMID:24813944</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
== References ==
== References ==
<references/>
<references/>

Revision as of 06:41, 21 May 2014

structure of UHRF2-SRA in complex with a 5hmC-containing DNA, complex I

4pw5, resolution 2.20Å

Drag the structure with the mouse to rotate

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