2qi9

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{{STRUCTURE_2qi9| PDB=2qi9 | SCENE= }}
{{STRUCTURE_2qi9| PDB=2qi9 | SCENE= }}
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'''ABC-transporter BtuCD in complex with its periplasmic binding protein BtuF'''
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===ABC-transporter BtuCD in complex with its periplasmic binding protein BtuF===
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==Overview==
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BtuCD is an adenosine triphosphate-binding cassette (ABC) transporter that translocates vitamin B12 from the periplasmic binding protein BtuF into the cytoplasm of Escherichia coli. The 2.6 angstrom crystal structure of a complex BtuCD-F reveals substantial conformational changes as compared with the previously reported structures of BtuCD and BtuF. The lobes of BtuF are spread apart, and B12 is displaced from the binding pocket. The transmembrane BtuC subunits reveal two distinct conformations, and the translocation pathway is closed to both sides of the membrane. Electron paramagnetic resonance spectra of spin-labeled cysteine mutants reconstituted in proteoliposomes are consistent with the conformation of BtuCD-F that was observed in the crystal structure. A comparison with BtuCD and the homologous HI1470/71 protein suggests that the structure of BtuCD-F may reflect a posttranslocation intermediate.
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(as it appears on PubMed at http://www.pubmed.gov), where 17673622 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17673622}}
==About this Structure==
==About this Structure==
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[[Category: Transmembrane]]
[[Category: Transmembrane]]
[[Category: Transport]]
[[Category: Transport]]
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Revision as of 21:07, 28 July 2008

Template:STRUCTURE 2qi9

ABC-transporter BtuCD in complex with its periplasmic binding protein BtuF

Template:ABSTRACT PUBMED 17673622

About this Structure

2QI9 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF., Hvorup RN, Goetz BA, Niederer M, Hollenstein K, Perozo E, Locher KP, Science. 2007 Sep 7;317(5843):1387-90. Epub 2007 Aug 2. PMID:17673622

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