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

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

doi:10.1002/prot.20751

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

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

Department of Pharmaceutical Sciences

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

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 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.

Original language	English
Pages (from-to)	322-328
Number of pages	7
Journal	Proteins: Structure, Function and Bioinformatics
Volume	62
Issue number	2
DOIs	https://doi.org/10.1002/prot.20751
State	Published - 1 Feb 2006

Keywords

Chlorobium tepidum
Chromosome partitioning
Crystal structure

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10.1002/prot.20751

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title = "Crystal structure of ScpB from Chlorobium tepidum, a protein involved in chromosome partitioning",

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 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.",

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T1 - Crystal structure of ScpB from Chlorobium tepidum, a protein involved in chromosome partitioning

AU - Kim, Jeong Sun

AU - Shin, Dong Hae

AU - Pufan, Ramona

AU - Huang, Candice

AU - Yokota, Hisao

AU - Kim, Rosalind

AU - Kim, Sung Hou

PY - 2006/2/1

Y1 - 2006/2/1

N2 - 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.

AB - 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.

KW - Chlorobium tepidum

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KW - Crystal structure

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

Abstract

Keywords

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