2mh9

From Proteopedia

Resonance assignment of RQC domain of human Bloom syndrome protein

PDB ID 2mh9

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Structural highlights

2mh9 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

RecQ C-terminal (RQC) domain is known as the main DNA binding module of RecQ helicases such as Bloom syndrome protein (BLM) and Werner syndrome protein (WRN) that recognizes various DNA structures. Even though BLM is able to resolve various DNA structures similarly to WRN, BLM has different binding preferences for DNA substrates from WRN. In this study, we determined the solution structure of the RQC domain of human BLM. The structure shares the common winged-helix motif with other RQC domains. However, half of the N-terminal has unstructured regions (alpha1-alpha2 loop and alpha3 region), and the aromatic side chain on the top of the beta-hairpin, which is important for DNA duplex strand separation in other RQC domains, is substituted with a negatively charged residue (D1165) followed by the polar residue (Q1166). The structurally distinctive features of the RQC domain of human BLM suggest that the DNA binding modes of the BLM RQC domain may be different from those of other RQC domains.

Solution structure of the RecQ C-terminal domain of human Bloom syndrome protein.,Park CJ, Ko J, Ryu KS, Choi BS J Biomol NMR. 2014 Feb;58(2):141-7. doi: 10.1007/s10858-014-9812-8. Epub 2014 Jan, 17. PMID:24435566^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Karow JK, Chakraverty RK, Hickson ID. The Bloom's syndrome gene product is a 3'-5' DNA helicase. J Biol Chem. 1997 Dec 5;272(49):30611-4. PMID:9388193
↑ Langland G, Elliott J, Li Y, Creaney J, Dixon K, Groden J. The BLM helicase is necessary for normal DNA double-strand break repair. Cancer Res. 2002 May 15;62(10):2766-70. PMID:12019152
↑ Nimonkar AV, Genschel J, Kinoshita E, Polaczek P, Campbell JL, Wyman C, Modrich P, Kowalczykowski SC. BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair. Genes Dev. 2011 Feb 15;25(4):350-62. doi: 10.1101/gad.2003811. PMID:21325134 doi:http://dx.doi.org/10.1101/gad.2003811
↑ Wan L, Han J, Liu T, Dong S, Xie F, Chen H, Huang J. Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair. Proc Natl Acad Sci U S A. 2013 Jun 25;110(26):10646-51. doi:, 10.1073/pnas.1220921110. Epub 2013 Mar 18. PMID:23509288 doi:http://dx.doi.org/10.1073/pnas.1220921110
↑ Park CJ, Ko J, Ryu KS, Choi BS. Solution structure of the RecQ C-terminal domain of human Bloom syndrome protein. J Biomol NMR. 2014 Feb;58(2):141-7. doi: 10.1007/s10858-014-9812-8. Epub 2014 Jan, 17. PMID:24435566 doi:http://dx.doi.org/10.1007/s10858-014-9812-8