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Crystal structure of ScpB from Chlorobium tepidum , a protein involved in chromosome partitioning
Author(s) -
Kim JeongSun,
Shin Dong Hae,
Pufan Ramona,
Huang Candice,
Yokota Hisao,
Kim Rosalind,
Kim SungHou
Publication year - 2005
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20751
Subject(s) - chromosome , genetics , gene , biology , dna , chemistry
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 β‐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. Proteins 2006. © 2005 Wiley‐Liss, Inc.