2iut | pdb_00002iut

P. aeruginosa FtsK motor domain, dimeric

spinqualitylabelsall models 2iut, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2iut is a 2 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AGS, MG Related: 2iuu, 2ius Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FTSK_PSEAE] Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Translocation stops specifically at Xer-dif sites, where FtsK interacts with the Xer recombinase, allowing activation of chromosome unlinking by recombination. FtsK orienting polar sequences (KOPS) guide the direction of DNA translocation. FtsK can remove proteins from DNA as it translocates, but translocation stops specifically at XerCD-dif site, thereby preventing removal of XerC and XerD from dif (Probable). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed FtsK is a DNA translocase that coordinates chromosome segregation and cell division in bacteria. In addition to its role as activator of XerCD site-specific recombination, FtsK can translocate double-stranded DNA (dsDNA) rapidly and directionally and reverse direction. We present crystal structures of the FtsK motor domain monomer, showing that it has a RecA-like core, the FtsK hexamer, and also showing that it is a ring with a large central annulus and a dodecamer consisting of two hexamers, head to head. Electron microscopy (EM) demonstrates the DNA-dependent existence of hexamers in solution and shows that duplex DNA passes through the middle of each ring. Comparison of FtsK monomer structures from two different crystal forms highlights a conformational change that we propose is the structural basis for a rotary inchworm mechanism of DNA translocation. Double-stranded DNA translocation: structure and mechanism of hexameric FtsK.,Massey TH, Mercogliano CP, Yates J, Sherratt DJ, Lowe J Mol Cell. 2006 Aug;23(4):457-69. PMID:16916635 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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