3vh5

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(New page: '''Unreleased structure''' The entry 3vh5 is ON HOLD Authors: Nishino, T., Takeuchi, K., Gascoigne, K.E., Suzuki, A., Hori, T., Oyama, T., Morikawa, K., Cheeseman, I.M., Fukagawa, T. D...)
Current revision (12:21, 8 November 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 3vh5 is ON HOLD
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==Crystal structure of the chicken CENP-T histone fold/CENP-W/CENP-S/CENP-X heterotetrameric complex, crystal form I==
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<StructureSection load='3vh5' size='340' side='right'caption='[[3vh5]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3vh5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VH5 FirstGlance]. <br>
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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]] 2.402&#8491;</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=3vh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vh5 OCA], [https://pdbe.org/3vh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vh5 RCSB], [https://www.ebi.ac.uk/pdbsum/3vh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vh5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CENPS_CHICK CENPS_CHICK] DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage (PubMed:20347428). In complex with CENPX (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM. In complex with CENPX and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks. In complex with CENPT, CENPW and CENPX (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression (PubMed:19620631). As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure. DNA-binding function is fulfilled in the presence of CENPX, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own (By similarity).[UniProtKB:Q8N2Z9]<ref>PMID:19620631</ref> <ref>PMID:20347428</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The multiprotein kinetochore complex must assemble at a specific site on each chromosome to achieve accurate chromosome segregation. Defining the nature of the DNA-protein interactions that specify the position of the kinetochore and provide a scaffold for kinetochore formation remain key goals. Here, we demonstrate that the centromeric histone-fold-containing CENP-T-W and CENP-S-X complexes coassemble to form a stable CENP-T-W-S-X heterotetramer. High-resolution structural analysis of the individual complexes and the heterotetramer reveals similarity to other histone fold-containing complexes including canonical histones within a nucleosome. The CENP-T-W-S-X heterotetramer binds to and supercoils DNA. Mutants designed to compromise heterotetramerization or the DNA-protein contacts around the heterotetramer strongly reduce the DNA binding and supercoiling activities in vitro and compromise kinetochore assembly in vivo. These data suggest that the CENP-T-W-S-X complex forms a unique nucleosome-like structure to generate contacts with DNA, extending the "histone code" beyond canonical nucleosome proteins.
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Authors: Nishino, T., Takeuchi, K., Gascoigne, K.E., Suzuki, A., Hori, T., Oyama, T., Morikawa, K., Cheeseman, I.M., Fukagawa, T.
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CENP-T-W-S-X Forms a Unique Centromeric Chromatin Structure with a Histone-like Fold.,Nishino T, Takeuchi K, Gascoigne KE, Suzuki A, Hori T, Oyama T, Morikawa K, Cheeseman IM, Fukagawa T Cell. 2012 Feb 3;148(3):487-501. PMID:22304917<ref>PMID:22304917</ref>
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Description: Crystal structure of the chicken CENP-T histone fold/CENP-W/CENP-S/CENP-X heterotetrameric complex, crystal form I
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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 3vh5" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Centromere protein|Centromere protein]]
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*[[Centromere protein 3D structure|Centromere protein 3D structure]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Gallus gallus]]
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[[Category: Large Structures]]
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[[Category: Cheeseman IM]]
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[[Category: Fukagawa T]]
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[[Category: Gascoigne KE]]
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[[Category: Hori T]]
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[[Category: Morikawa K]]
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[[Category: Nishino T]]
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[[Category: Oyama T]]
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[[Category: Suzuki A]]
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[[Category: Takeuchi K]]

Current revision

Crystal structure of the chicken CENP-T histone fold/CENP-W/CENP-S/CENP-X heterotetrameric complex, crystal form I

PDB ID 3vh5

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