1t98

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[[Image:1t98.gif|left|200px]]
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{{STRUCTURE_1t98| PDB=1t98 | SCENE= }}
{{STRUCTURE_1t98| PDB=1t98 | SCENE= }}
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'''Crystal Structure of MukF(1-287)'''
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===Crystal Structure of MukF(1-287)===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15902272 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15902272}}
==About this Structure==
==About this Structure==
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[[Category: Helix-turn helix]]
[[Category: Helix-turn helix]]
[[Category: Winged helix]]
[[Category: Winged helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:41:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:19:35 2008''

Revision as of 11:19, 29 July 2008

Image:1t98.png

Template:STRUCTURE 1t98

Crystal Structure of MukF(1-287)

Template:ABSTRACT PUBMED 15902272

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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