Crystal structure of ScpB from Chlorobium tepidum, a protein involved in chromosome partitioning |
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Authors: | Kim Jeong-Sun Shin Dong Hae Pufan Ramona Huang Candice Yokota Hisao Kim Rosalind Kim Sung-Hou |
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Affiliation: | Department of Chemistry, University of California, Berkeley, California 94720, USA. |
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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. |
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Keywords: | crystal structure Chlorobium tepidum chromosome partitioning |
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