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4s3h

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<StructureSection load='4s3h' size='340' side='right'caption='[[4s3h]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='4s3h' size='340' side='right'caption='[[4s3h]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4s3h]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S3H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S3H FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4s3h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S3H FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.701&#8491;</td></tr>
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<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=4s3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s3h OCA], [http://pdbe.org/4s3h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4s3h RCSB], [http://www.ebi.ac.uk/pdbsum/4s3h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4s3h ProSAT]</span></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=SO4:SULFATE+ION'>SO4</scene></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=4s3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s3h OCA], [https://pdbe.org/4s3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s3h RCSB], [https://www.ebi.ac.uk/pdbsum/4s3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s3h ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/MDB1_SCHPO MDB1_SCHPO]
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MDC1 is a key factor of DNA damage response in mammalian cells. It possesses two phospho-binding domains. In its C-terminus, a tandem BRCA1 C-terminal (tBRCT) domain binds phosphorylated histone H2AX, and in its N-terminus, a forkhead-associated (FHA) domain mediates a phosphorylation-enhanced homodimerization. The FHA domain of the Drosophila homolog of MDC1, MU2, also forms a homodimer but utilizes a different dimer interface. The functional importance of the dimerization of MDC1-family proteins is uncertain. In the fission yeast Schizosaccharomyces pombe, a protein sharing homology with MDC1 in the tBRCT domain, Mdb1, regulates DNA damage response and mitotic spindle functions. Here, we report the crystal structure of the N-terminal 91 amino acids of Mdb1. Despite a lack of obvious sequence conservation to the FHA domain of MDC1, this region of Mdb1 adopts an FHA-like fold and is therefore termed Mdb1-FHA. Unlike canonical FHA domains, Mdb1-FHA lacks all the conserved phospho-binding residues. It forms a stable homodimer through an interface distinct from those of MDC1 and MU2. Mdb1-FHA is important for the localization of Mdb1 to DNA damage sites and the spindle midzone, contributes to the roles of Mdb1 in cellular responses to genotoxins and an antimicrotubule drug, and promotes in-vitro binding of Mdb1 to a phospho-H2A peptide. The defects caused by the loss of Mdb1-FHA can be rescued by fusion with either of two heterologous dimerization domains, suggesting that the main function of Mdb1-FHA is mediating dimerization. Our data support that FHA-mediated dimerization is conserved for MDC1-family proteins.
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Dimerization mediated by a divergent FHA domain is essential for the DNA damage and spindle functions of fission yeast Mdb1.,Luo S, Xin X, Du LL, Ye K, Wei Y J Biol Chem. 2015 Jul 9. pii: jbc.M115.642538. PMID:26160178<ref>PMID:26160178</ref>
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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 4s3h" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fission yeast]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Luo, S]]
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[[Category: Schizosaccharomyces pombe 972h-]]
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[[Category: Ye, K]]
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[[Category: Luo S]]
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[[Category: Dimerization]]
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[[Category: Ye K]]
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[[Category: Mdb1]]
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[[Category: Unknown function]]
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Current revision

Crystal structure of S. pombe Mdb1 FHA domain

PDB ID 4s3h

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