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Crystal structure of ScpB from Chlorobium tepidum, a protein involved in chromosome partitioning.

作者信息

Kim Jeong-Sun, Shin Dong Hae, Pufan Ramona, Huang Candice, Yokota Hisao, Kim Rosalind, Kim Sung-Hou

机构信息

Department of Chemistry, University of California, Berkeley, California 94720, USA.

出版信息

Proteins. 2006 Feb 1;62(2):322-8. doi: 10.1002/prot.20751.

DOI:10.1002/prot.20751
PMID:16294331
Abstract

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.

摘要

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