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| {{STRUCTURE_3b5w| PDB=3b5w | SCENE= }} | | {{STRUCTURE_3b5w| PDB=3b5w | SCENE= }} |
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| '''Crystal Structure of Eschericia coli MsbA'''
| | ===Crystal Structure of Eschericia coli MsbA=== |
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| ==Overview==
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| ATP-binding cassette (ABC) transporters are integral membrane proteins that translocate a wide variety of substrates across cellular membranes and are conserved from bacteria to humans. Here we compare four x-ray structures of the bacterial ABC lipid flippase, MsbA, trapped in different conformations, two nucleotide-bound structures and two in the absence of nucleotide. Comparison of the nucleotide-free conformations of MsbA reveals a flexible hinge formed by extracellular loops 2 and 3. This hinge allows the nucleotide-binding domains to disassociate while the ATP-binding half sites remain facing each other. The binding of the nucleotide causes a packing rearrangement of the transmembrane helices and changes the accessibility of the transporter from cytoplasmic (inward) facing to extracellular (outward) facing. The inward and outward openings are mediated by two different sets of transmembrane helix interactions. Altogether, the conformational changes between these structures suggest that large ranges of motion may be required for substrate transport.
| | The line below this paragraph, {{ABSTRACT_PUBMED_18024585}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18024585 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18024585}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Nucleotide-binding]] | | [[Category: Nucleotide-binding]] |
| [[Category: Transmembrane]] | | [[Category: Transmembrane]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:25:25 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:14:55 2008'' |
