3b60

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{{STRUCTURE_3b60| PDB=3b60 | SCENE= }}
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'''Crystal Structure of MsbA from Salmonella typhimurium with AMPPNP, higher resolution form'''
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===Crystal Structure of MsbA from Salmonella typhimurium with AMPPNP, higher resolution form===
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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.
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==About this Structure==
==About this Structure==
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[[Category: Nucleotide-binding]]
[[Category: Nucleotide-binding]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:01:20 2008''

Revision as of 04:01, 29 July 2008

Image:3b60.png

Template:STRUCTURE 3b60

Crystal Structure of MsbA from Salmonella typhimurium with AMPPNP, higher resolution form

Template:ABSTRACT PUBMED 18024585

About this Structure

3B60 is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

Flexibility in the ABC transporter MsbA: Alternating access with a twist., Ward A, Reyes CL, Yu J, Roth CB, Chang G, Proc Natl Acad Sci U S A. 2007 Nov 27;104(48):19005-10. Epub 2007 Nov 16. PMID:18024585

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