1e69

<table><tr><td colspan='2'>[[1e69]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E69 FirstGlance]. <br>

</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=1e69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e69 OCA], [https://pdbe.org/1e69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e69 RCSB], [https://www.ebi.ac.uk/pdbsum/1e69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e69 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/Q9X0R4_THEMA Q9X0R4_THEMA]] Required for chromosome condensation and partitioning.[HAMAP-Rule:MF_01894]

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== Publication Abstract from PubMed ==

SMC (structural maintenance of chromosomes) proteins are large coiled-coil proteins involved in chromosome condensation, sister chromatid cohesion, and DNA double-strand break processing. They share a conserved five-domain architecture with three globular domains separated by two long coiled-coil segments. The coiled-coil segments are antiparallel, bringing the N and C-terminal globular domains together. We have expressed a fusion protein of the N and C-terminal globular domains of Thermotoga maritima SMC in Escherichia coli by replacing the approximately 900 residue coiled-coil and hinge segment with a short peptide linker. The SMC head domain (SMChd) binds and condenses DNA in an ATP-dependent manner. Using selenomethionine-substituted protein and multiple anomalous dispersion phasing, we have solved the crystal structure of the SMChd to 3.1 A resolution. In the monoclinic crystal form, six SMChd molecules form two turns of a helix. The fold of SMChd is closely related to the ATP-binding cassette (ABC) ATPase family of proteins and Rad50, a member of the SMC family involved in DNA double-strand break repair. In SMChd, the ABC ATPase fold is formed by the N and C-terminal domains with the 900 residue coiled-coil and hinge segment inserted in the middle of the fold. The crystal structure of an SMChd confirms that the coiled-coil segments in SMC proteins are anti-parallel and shows how the N and C-terminal domains come together to form an ABC ATPase. Comparison to the structure of the MukB N-terminal domain demonstrates the close relationship between MukB and SMC proteins, and indicates a helix to strand conversion when N and C-terminal parts come together.

Crystal structure of the SMC head domain: an ABC ATPase with 900 residues antiparallel coiled-coil inserted.,Lowe J, Cordell SC, van den Ent F J Mol Biol. 2001 Feb 9;306(1):25-35. PMID:11178891<ref>PMID:11178891</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Atcc 43589]]

[[Category: Cordell, S C]]

[[Category: Ent, F van den]]

[[Category: Lowe, J]]

[[Category: Chromosome segregation]]

[[Category: Structural maintenance of chromosome]]