3IBP image
Deposition Date 2009-07-16
Release Date 2010-01-26
Last Version Date 2024-11-20
Entry Detail
PDB ID:
3IBP
Keywords:
Title:
The Crystal Structure of the Dimerization Domain of Escherichia coli Structural Maintenance of Chromosomes Protein MukB
Biological Source:
Source Organism(s):
Expression System(s):
Method Details:
Experimental Method:
Resolution:
3.10 Å
R-Value Free:
0.27
R-Value Work:
0.24
R-Value Observed:
0.24
Space Group:
P 43 2 2
Macromolecular Entities
Polymer Type:polypeptide(L)
Molecule:Chromosome partition protein
Gene (Uniprot):mukB
Chain IDs:A
Chain Length:302
Number of Molecules:1
Biological Source:Escherichia coli
Modified Residue
Compound ID Chain ID Parent Comp ID Details 2D Image
MSE A MET SELENOMETHIONINE
Ligand Molecules
Primary Citation
The crystal structure of the hinge domain of the Escherichia coli structural maintenance of chromosomes protein MukB.
J. Mol. Biol. 395 11 19 (2010)
PMID: 19853611 DOI: 10.1016/j.jmb.2009.10.040

Abstact

MukB, a divergent structural maintenance of chromosomes (SMC) protein, is important for chromosomal segregation and condensation in gamma-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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Chemical

Disease

Primary Citation of related structures
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