Crystal structure of ScpB from Chlorobium tepidum, a protein involved in chromosome partitioning.
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.
Kim
Jeong-Sun
JS
Department of Chemistry, University of California, Berkeley, California 94720, USA.
Shin
Dong Hae
DH
Pufan
Ramona
R
Huang
Candice
C
Yokota
Hisao
H
Kim
Rosalind
R
Kim
Sung-Hou
SH
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics*; D041883:Chlorobium / Q000235:genetics*; D002876:Chromosomes, Bacterial / Q000235:genetics; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins