1t6s | pdb_00001t6s

Crystal structure of a conserved hypothetical protein from Chlorobium tepidum

spinqualitylabelsall models 1t6s, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1t6s is a 2 chain structure with sequence from Chlte. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NO3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function [Q8KF54_CHLTE] Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves (By similarity). 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 Structural maintenance of chromosome (SMC) proteins are essential in chromosome condensation and interact with non-SMC proteins in eukaryotes and with segregation and condensation proteins (ScpA and ScpB) in prokaryotes. The highly conserved gene in Chlorobium tepidum gi 21646405 encodes ScpB (ScpB_ChTe). The high resolution crystal structure of ScpB_ChTe shows that the monomeric structure consists of two similarly shaped globular domains composed of three helices sided by beta-strands [a winged helix-turn-helix (HTH)], a motif observed in the C-terminal domain of Scc1, a functionally related eukaryotic ScpA homolog, as well as in many DNA binding proteins. Crystal structure of ScpB from Chlorobium tepidum, a protein involved in chromosome partitioning.,Kim JS, Shin DH, Pufan R, Huang C, Yokota H, Kim R, Kim SH Proteins. 2006 Feb 1;62(2):322-8. PMID:16294331 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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