2nq2: Difference between revisions

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[[Image:2nq2.gif|left|200px]]
{{Seed}}
[[Image:2nq2.png|left|200px]]


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{{STRUCTURE_2nq2|  PDB=2nq2  |  SCENE=  }}  
{{STRUCTURE_2nq2|  PDB=2nq2  |  SCENE=  }}  


'''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==
==About this Structure==
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[[Category: Putative iron chelatin abc transporter]]
[[Category: Putative iron chelatin abc transporter]]
[[Category: Transmembrane domain]]
[[Category: Transmembrane domain]]
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