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5bnv

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Revision as of 14:13, 24 May 2017

Crystal structure of Human MCM2 HBD chaperoning a histone H3-H4 tetramer

Structural highlights

5bnv is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	5bnx, 5bo0
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MCM2_HUMAN] Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division.^[1]

Publication Abstract from PubMed

During DNA replication, chromatin is reassembled by recycling of modified old histones and deposition of new ones. How histone dynamics integrates with DNA replication to maintain genome and epigenome information remains unclear. Here, we reveal how human MCM2, part of the replicative helicase, chaperones histones H3-H4. Our first structure shows an H3-H4 tetramer bound by two MCM2 histone-binding domains (HBDs), which hijack interaction sites used by nucleosomal DNA. Our second structure reveals MCM2 and ASF1 cochaperoning an H3-H4 dimer. Mutational analyses show that the MCM2 HBD is required for MCM2-7 histone-chaperone function and normal cell proliferation. Further, we show that MCM2 can chaperone both new and old canonical histones H3-H4 as well as H3.3 and CENPA variants. The unique histone-binding mode of MCM2 thus endows the replicative helicase with ideal properties for recycling histones genome wide during DNA replication.

A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks.,Huang H, Stromme CB, Saredi G, Hodl M, Strandsby A, Gonzalez-Aguilera C, Chen S, Groth A, Patel DJ Nat Struct Mol Biol. 2015 Jul 13. doi: 10.1038/nsmb.3055. PMID:26167883^[2]

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

References

↑ Todorov IT, Pepperkok R, Philipova RN, Kearsey SE, Ansorge W, Werner D. A human nuclear protein with sequence homology to a family of early S phase proteins is required for entry into S phase and for cell division. J Cell Sci. 1994 Jan;107 ( Pt 1):253-65. PMID:8175912
↑ Huang H, Stromme CB, Saredi G, Hodl M, Strandsby A, Gonzalez-Aguilera C, Chen S, Groth A, Patel DJ. A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks. Nat Struct Mol Biol. 2015 Jul 13. doi: 10.1038/nsmb.3055. PMID:26167883 doi:http://dx.doi.org/10.1038/nsmb.3055

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5bnv"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Human MCM2 HBD chaperoning a histone H3-H4 tetramer==
 <StructureSection load='5bnv' size='340' side='right' caption='[[5bnv]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bnx|5bnx]], [[5bo0|5bo0]]</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=5bnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bnv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5bnv RCSB], [http://www.ebi.ac.uk/pdbsum/5bnv PDBsum]</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=5bnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bnv OCA], [http://pdbe.org/5bnv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bnv RCSB], [http://www.ebi.ac.uk/pdbsum/5bnv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bnv ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 5bnv" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

5bnv

From Proteopedia

Revision as of 14:13, 24 May 2017

Crystal structure of Human MCM2 HBD chaperoning a histone H3-H4 tetramer

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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