2nq2: Difference between revisions

Revision as of 11:02, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2nq2.png

Template:STRUCTURE 2nq2

An inward-facing conformation of a putative metal-chelate type ABC transporter.An inward-facing conformation of a putative metal-chelate type ABC transporter.

Template:ABSTRACT PUBMED 17158291

About this StructureAbout this Structure

2NQ2 is a Protein complex structure of sequences from Haemophilus influenzae. Full crystallographic information is available from OCA.

ReferenceReference

An inward-facing conformation of a putative metal-chelate-type ABC transporter., Pinkett HW, Lee AT, Lum P, Locher KP, Rees DC, Science. 2007 Jan 19;315(5810):373-7. Epub 2006 Dec 7. PMID:17158291

Page seeded by OCA on Mon Jul 28 11:02:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''An inward-facing conformation of a putative metal-chelate type ABC transporter.'''
+===An inward-facing conformation of a putative metal-chelate type ABC transporter.===
-==Overview==
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-The crystal structure of a putative metal-chelate-type adenosine triphosphate (ATP)-binding cassette (ABC) transporter encoded by genes HI1470 and HI1471 of Haemophilus influenzae has been solved at 2.4 angstrom resolution. The permeation pathway exhibits an inward-facing conformation, in contrast to the outward-facing state previously observed for the homologous vitamin B12 importer BtuCD. Although the structures of both HI1470/1 and BtuCD have been solved in nucleotide-free states, the pairs of ABC subunits in these two structures differ by a translational shift in the plane of the membrane that coincides with a repositioning of the membrane-spanning subunits. The differences observed between these ABC transporters involve relatively modest rearrangements and may serve as structural models for inward- and outward-facing conformations relevant to the alternating access mechanism of substrate translocation.
+The line below this paragraph, {{ABSTRACT_PUBMED_17158291}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17158291 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17158291}}
 ==About this Structure==
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 [[Category: Putative iron chelatin abc transporter]]
 [[Category: Transmembrane domain]]
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