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==Structure of BLM RQC domain bound to an arsenate ion== | |||
<StructureSection load='3we3' size='340' side='right' caption='[[3we3]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3we3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WE3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WE3 FirstGlance]. <br> | |||
==Disease== | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ART:ARSENATE'>ART</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3we2|3we2]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BLM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=3we3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3we3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3we3 RCSB], [http://www.ebi.ac.uk/pdbsum/3we3 PDBsum]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[[http://www.uniprot.org/uniprot/BLM_HUMAN BLM_HUMAN]] Bloom syndrome. The disease is caused by mutations affecting the gene represented in this entry. | [[http://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== | |||
[[http://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> | [[http://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> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: DNA helicase]] | [[Category: DNA helicase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Hakoshima, T | [[Category: Hakoshima, T]] | ||
[[Category: Kim, S Y | [[Category: Kim, S Y]] | ||
[[Category: Kitano, K | [[Category: Kitano, K]] | ||
[[Category: Dna binding]] | [[Category: Dna binding]] | ||
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Dna helicase]] | [[Category: Dna helicase]] | ||
[[Category: Winged-helix]] | [[Category: Winged-helix]] | ||
Revision as of 20:20, 21 December 2014
Structure of BLM RQC domain bound to an arsenate ionStructure of BLM RQC domain bound to an arsenate ion
Structural highlights
Disease[BLM_HUMAN] Bloom syndrome. The disease is caused by mutations affecting the gene represented in this entry. Function[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).[1] [2] [3] [4] Publication Abstract from PubMedBloom 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. 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[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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