3b5w

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[[Image:3b5w.jpg|left|200px]]
[[Image:3b5w.jpg|left|200px]]
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{{Structure
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|PDB= 3b5w |SIZE=350|CAPTION= <scene name='initialview01'>3b5w</scene>, resolution 5.300&Aring;
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The line below this paragraph, containing "STRUCTURE_3b5w", creates the "Structure Box" on the page.
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|SITE=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= msbA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_3b5w| PDB=3b5w | SCENE= }}
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|RELATEDENTRY=[[3b5x|3B5X]], [[3b5y|3B5Y]], [[3b5z|3B5Z]], [[3b60|3B60]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b5w OCA], [http://www.ebi.ac.uk/pdbsum/3b5w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3b5w RCSB]</span>
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}}
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'''Crystal Structure of Eschericia coli MsbA'''
'''Crystal Structure of Eschericia coli MsbA'''
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[[Category: Ward, A.]]
[[Category: Ward, A.]]
[[Category: Yu, J.]]
[[Category: Yu, J.]]
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[[Category: abc transporter]]
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[[Category: Abc transporter]]
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[[Category: atp-binding]]
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[[Category: Atp-binding]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: inner membrane]]
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[[Category: Inner membrane]]
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[[Category: lipid flippase]]
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[[Category: Lipid flippase]]
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[[Category: lipid transport]]
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[[Category: Lipid transport]]
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[[Category: membrane]]
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[[Category: Membrane]]
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[[Category: membrane protein]]
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[[Category: Membrane protein]]
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[[Category: msba]]
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[[Category: Msba]]
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[[Category: nucleotide-binding]]
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[[Category: Nucleotide-binding]]
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[[Category: transmembrane]]
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[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:25:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:23:16 2008''
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Revision as of 17:25, 4 May 2008

Template:STRUCTURE 3b5w

Crystal Structure of Eschericia coli MsbA


Overview

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.

About this Structure

3B5W is a Single protein structure of sequence from Escherichia coli. 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 Page seeded by OCA on Sun May 4 20:25:25 2008

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