3v9r

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Crystal structure of Saccharomyces cerevisiae MHF complex

Structural highlights

3v9r is a 4 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:MSE, SO4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CENPS_YEAST dsDNA-binding component of a FANCM-MHF complex involved in DNA damage repair and genome maintenance (PubMed:20347428). FANCM-MHF promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork (By similarity). Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly (PubMed:22561346).[UniProtKB:O74896][1] [2]

Publication Abstract from PubMed

Fanconi anemia (FA) is a chromosomal instability disorder associated with deficiencies in the Fanconi anemia complementation group (FANC) network. A complex consisting of FANCM-associated histone-fold proteins 1 and 2 (MHF1 and MHF2) has been shown to act cooperatively with FANCM in DNA damage repair in the FA pathway. Here we report the structure of Saccharomyces cerevisiae MHF complex in which MHF1 and MHF2 assume a typical histone fold, and the complex has a heterotetrameric architecture similar to that of the histones (H3-H4)(2) heterotetramer. Loop L2 of MHF1 is probably involved in DNA binding, and loop L3 and helices alpha2 and alpha3 of one MHF1 subunit interact with those of the other to form two heterotetramer interfaces. Further genetic data demonstrate that the heterotetramer assembly is essential for the function of the complex in DNA repair. These results provide, to the best of our knowledge, new mechanistic insights into the function of the MHF complex.

Saccharomyces Cerevisiae MHF Complex Structurally Resembles the Histones (H3-H4)(2) Heterotetramer and Functions as a Heterotetramer.,Yang H, Zhang T, Tao Y, Wu L, Li HT, Zhou JQ, Zhong C, Ding J Structure. 2012 Feb 8;20(2):364-70. PMID:22325783[3]

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

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References

  1. ↑ Yan Z, Delannoy M, Ling C, Daee D, Osman F, Muniandy PA, Shen X, Oostra AB, Du H, Steltenpool J, Lin T, Schuster B, Décaillet C, Stasiak A, Stasiak AZ, Stone S, Hoatlin ME, Schindler D, Woodcock CL, Joenje H, Sen R, de Winter JP, Li L, Seidman MM, Whitby MC, Myung K, Constantinou A, Wang W. A histone-fold complex and FANCM form a conserved DNA-remodeling complex to maintain genome stability. Mol Cell. 2010 Mar 26;37(6):865-78. PMID:20347428 doi:10.1016/j.molcel.2010.01.039
  2. ↑ Schleiffer A, Maier M, Litos G, Lampert F, Hornung P, Mechtler K, Westermann S. CENP-T proteins are conserved centromere receptors of the Ndc80 complex. Nat Cell Biol. 2012 May 6;14(6):604-13. doi: 10.1038/ncb2493. PMID:22561346 doi:http://dx.doi.org/10.1038/ncb2493
  3. ↑ Yang H, Zhang T, Tao Y, Wu L, Li HT, Zhou JQ, Zhong C, Ding J. Saccharomyces Cerevisiae MHF Complex Structurally Resembles the Histones (H3-H4)(2) Heterotetramer and Functions as a Heterotetramer. Structure. 2012 Feb 8;20(2):364-70. PMID:22325783 doi:10.1016/j.str.2011.12.012

Contents


PDB ID 3v9r

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OCA

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