The Crystal Structure of the Hinge Domain of the Escherichia coli Structural Maintenance of Chromosomes Protein MukB

Yinyin Li, Allyn J. Schoeffler, James M Berger, Martha G. Oakley

Research output: Contribution to journalArticle

Abstract

MukB, a divergent structural maintenance of chromosomes (SMC) protein, is important for chromosomal segregation and condensation in γ-proteobacteria. MukB and canonical SMC proteins share a characteristic five-domain structure. Globular N- and C-terminal domains interact to form an ATP-binding cassette-like ATPase or "head" domain, which is connected to a smaller dimerization or "hinge" domain by a long, antiparallel coiled coil. In addition to mediating dimerization, this hinge region has been implicated in both conformational flexibility and dynamic protein-DNA interactions. We report here the first crystallographic model of the MukB hinge domain. This model also contains approximately 20% of the coiled-coil domain, including an unusual coiled-coil deviation. These results will facilitate studies to clarify the roles of both the hinge and the coiled-coil domains in MukB function.

Original languageEnglish (US)
Pages (from-to)11-19
Number of pages9
JournalJournal of Molecular Biology
Volume395
Issue number1
DOIs
StatePublished - Jan 8 2010
Externally publishedYes

Fingerprint

Chromosomes
Maintenance
Dimerization
Escherichia coli
Proteobacteria
Proteins
Adenosine Triphosphatases
Adenosine Triphosphate
Head
DNA

Keywords

  • coiled coil
  • condensin
  • hinge
  • MukB
  • structural maintenance of chromosomes (SMC)

ASJC Scopus subject areas

  • Molecular Biology

Cite this

The Crystal Structure of the Hinge Domain of the Escherichia coli Structural Maintenance of Chromosomes Protein MukB. / Li, Yinyin; Schoeffler, Allyn J.; Berger, James M; Oakley, Martha G.

In: Journal of Molecular Biology, Vol. 395, No. 1, 08.01.2010, p. 11-19.

Research output: Contribution to journalArticle

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N2 - MukB, a divergent structural maintenance of chromosomes (SMC) protein, is important for chromosomal segregation and condensation in γ-proteobacteria. MukB and canonical SMC proteins share a characteristic five-domain structure. Globular N- and C-terminal domains interact to form an ATP-binding cassette-like ATPase or "head" domain, which is connected to a smaller dimerization or "hinge" domain by a long, antiparallel coiled coil. In addition to mediating dimerization, this hinge region has been implicated in both conformational flexibility and dynamic protein-DNA interactions. We report here the first crystallographic model of the MukB hinge domain. This model also contains approximately 20% of the coiled-coil domain, including an unusual coiled-coil deviation. These results will facilitate studies to clarify the roles of both the hinge and the coiled-coil domains in MukB function.

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