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3we2

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Current revision (08:44, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3we2' size='340' side='right'caption='[[3we2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='3we2' size='340' side='right'caption='[[3we2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3we2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WE2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3we2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WE2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3we3|3we3]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BLM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3we2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3we2 OCA], [https://pdbe.org/3we2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3we2 RCSB], [https://www.ebi.ac.uk/pdbsum/3we2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3we2 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=3we2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3we2 OCA], [https://pdbe.org/3we2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3we2 RCSB], [https://www.ebi.ac.uk/pdbsum/3we2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3we2 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/BLM_HUMAN BLM_HUMAN]] Bloom syndrome. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/BLM_HUMAN BLM_HUMAN] Bloom syndrome. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/BLM_HUMAN BLM_HUMAN]] Participates in DNA replication and repair. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction. Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA. Negatively regulates sister chromatid exchange (SCE).<ref>PMID:9388193</ref> <ref>PMID:12019152</ref> <ref>PMID:21325134</ref> <ref>PMID:23509288</ref>
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[https://www.uniprot.org/uniprot/BLM_HUMAN BLM_HUMAN] Participates in DNA replication and repair. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction. Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA. Negatively regulates sister chromatid exchange (SCE).<ref>PMID:9388193</ref> <ref>PMID:12019152</ref> <ref>PMID:21325134</ref> <ref>PMID:23509288</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bloom syndrome is a rare genetic disorder characterized by genomic instability and cancer predisposition. The disease is caused by mutations of the Bloom syndrome protein (BLM). Here we report the crystal structure of a RecQ C-terminal (RQC) domain from human BLM. The structure reveals three novel features of BLM RQC which distinguish it from the previous structures of the Werner syndrome protein (WRN) and RECQ1. First, BLM RQC lacks an aromatic residue at the tip of the beta-wing, a key element of the RecQ-family helicases used for DNA-strand separation. Second, a BLM-specific insertion between the N-terminal helices exhibits a looping-out structure that extends at right angles to the beta-wing. Deletion mutagenesis of this insertion interfered with binding to Holliday junction. Third, the C-terminal region of BLM RQC adopts an extended structure running along the domain surface, which may facilitate the spatial positioning of an HRDC domain in the full-length protein.
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Structure of the RecQ C-terminal Domain of Human Bloom Syndrome Protein.,Kim SY, Hakoshima T, Kitano K Sci Rep. 2013 Nov 21;3:3294. doi: 10.1038/srep03294. PMID:24257077<ref>PMID:24257077</ref>
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==See Also==
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*[[Helicase 3D structures|Helicase 3D structures]]
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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 3we2" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: DNA helicase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hakoshima, T]]
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[[Category: Hakoshima T]]
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[[Category: Kim, S Y]]
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[[Category: Kim SY]]
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[[Category: Kitano, K]]
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[[Category: Kitano K]]
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[[Category: Dna binding]]
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[[Category: Dna binding protein]]
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[[Category: Dna helicase]]
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[[Category: Winged-helix]]
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Current revision

Structure of BLM RQC domain bound to a phosphate ion

PDB ID 3we2

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