5xg2: Difference between revisions

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 ==Crystal structure of a coiled-coil segment (residues 345-468 and 694-814) of Pyrococcus yayanosii Smc==
-<StructureSection load='5xg2' size='340' side='right' caption='[[5xg2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='5xg2' size='340' side='right'caption='[[5xg2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5xg2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XG2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XG2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5xg2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_yayanosii_CH1 Pyrococcus yayanosii CH1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XG2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
+</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&#8491;</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=5xg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xg2 OCA], [http://pdbe.org/5xg2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xg2 RCSB], [http://www.ebi.ac.uk/pdbsum/5xg2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xg2 ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=5xg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xg2 OCA], [https://pdbe.org/5xg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xg2 RCSB], [https://www.ebi.ac.uk/pdbsum/5xg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xg2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/F8AFS8_PYRYC F8AFS8_PYRYC]] Required for chromosome condensation and partitioning.[HAMAP-Rule:MF_01894]
+[https://www.uniprot.org/uniprot/F8AFS8_PYRYC F8AFS8_PYRYC] Required for chromosome condensation and partitioning.[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>
+==See Also==
+*[[Condensin|Condensin]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5xg2" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Lee, H]]
+[[Category: Large Structures]]
-[[Category: Noh, H]]
+[[Category: Pyrococcus yayanosii CH1]]
-[[Category: Oh, B H]]
+[[Category: Lee H]]
-[[Category: Coiled-coil]]
+[[Category: Noh H]]
-[[Category: Dna binding protein]]
+[[Category: Oh B-H]]
-[[Category: Prokaryotic condensin]]
-[[Category: Smc]]