2nq2: Difference between revisions
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<StructureSection load='2nq2' size='340' side='right' caption='[[2nq2]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2nq2' size='340' side='right' caption='[[2nq2]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2nq2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2nq2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NQ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NQ2 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HI_1471 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HI_1471 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896]), HI_1470 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nq2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2nq2 RCSB], [http://www.ebi.ac.uk/pdbsum/2nq2 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nq2 OCA], [http://pdbe.org/2nq2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nq2 RCSB], [http://www.ebi.ac.uk/pdbsum/2nq2 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2nq2" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacterium influenzae lehmann and neumann 1896]] | ||
[[Category: Lee, A T]] | [[Category: Lee, A T]] | ||
[[Category: Locher, K P]] | [[Category: Locher, K P]] | ||
Revision as of 22:39, 10 September 2015
An inward-facing conformation of a putative metal-chelate type ABC transporter.An inward-facing conformation of a putative metal-chelate type ABC transporter.
Structural highlights
Function[Y1471_HAEIN] Probably part of a binding-protein-dependent transport system. Probably responsible for the translocation of the substrate across the membrane. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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