1t98
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(New page: 200px<br /><applet load="1t98" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t98, resolution 2.90Å" /> '''Crystal Structure of...)
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Revision as of 00:58, 21 November 2007
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Crystal Structure of MukF(1-287)
Overview
The Escherichia coli MukB, MukE, and MukF proteins form a bacterial, condensin (MukBEF) that contributes to chromosome management by compacting, DNA. MukB is an ATPase and DNA-binding protein of the SMC superfamily;, however, the structure and function of non-SMC components, such as MukF, have been less forthcoming. Here, we report the crystal structure of the, N-terminal 287 amino acids of MukF at 2.9 A resolution. This region folds, into a winged-helix domain and an extended coiled-coil domain that, self-associate to form a stable, doubly domain-swapped dimer. Protein, dissection and affinity purification data demonstrate that the region of, MukF C-terminal to this fragment binds to MukE and MukB. Our findings, together with sequence analyses, indicate that MukF is a kleisin subunit, for E. coli condensin and suggest a means by which it may organize the, MukBEF assembly.
About this Structure
1T98 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The MukF subunit of Escherichia coli condensin: architecture and functional relationship to kleisins., Fennell-Fezzie R, Gradia SD, Akey D, Berger JM, EMBO J. 2005 Jun 1;24(11):1921-30. Epub 2005 May 19. PMID:15902272
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