View source for 5xns


==Crystal structure of the Smc head domain with an extended coiled coil bound to the C-terminal domain of ScpA derived from Pyrococcus furiosus==
<StructureSection load='5xns' size='340' side='right'caption='[[5xns]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xns]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XNS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xns OCA], [https://pdbe.org/5xns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xns RCSB], [https://www.ebi.ac.uk/pdbsum/5xns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xns ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SMC_PYRFU SMC_PYRFU] Required for chromosome condensation and partitioning (By similarity). Binds single-stranded but not double-stranded DNA.[HAMAP-Rule:MF_01894]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Multi-subunit SMC complexes control chromosome superstructure and promote chromosome disjunction, conceivably by actively translocating along DNA double helices. SMC subunits comprise an ABC ATPase "head" and a "hinge" dimerization domain connected by a 49 nm coiled-coil "arm." The heads undergo ATP-dependent engagement and disengagement to drive SMC action on the chromosome. Here, we elucidate the architecture of prokaryotic Smc dimers by high-throughput cysteine cross-linking and crystallography. Co-alignment of the Smc arms tightly closes the interarm space and misaligns the Smc head domains at the end of the rod by close apposition of their ABC signature motifs. Sandwiching of ATP molecules between Smc heads requires them to substantially tilt and translate relative to each other, thereby opening up the Smc arms. We show that this mechanochemical gating reaction regulates chromosome targeting and propose a mechanism for DNA translocation based on the merging of DNA loops upon closure of Smc arms.

Structure of Full-Length SMC and Rearrangements Required for Chromosome Organization.,Diebold-Durand ML, Lee H, Ruiz Avila LB, Noh H, Shin HC, Im H, Bock FP, Burmann F, Durand A, Basfeld A, Ham S, Basquin J, Oh BH, Gruber S Mol Cell. 2017 Jul 20;67(2):334-347.e5. doi: 10.1016/j.molcel.2017.06.010. Epub, 2017 Jul 6. PMID:28689660<ref>PMID:28689660</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xns" style="background-color:#fffaf0;"></div>

==See Also==
*[[Condensin|Condensin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus DSM 3638]]
[[Category: Kwak M-J]]
[[Category: Oh B-H]]
[[Category: Shin H-C]]