2nq2
From Proteopedia
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| - | [[Image:2nq2.gif|left|200px]] | ||
| - | + | ==An inward-facing conformation of a putative metal-chelate type ABC transporter.== | |
| - | + | <StructureSection load='2nq2' size='340' side='right'caption='[[2nq2]], [[Resolution|resolution]] 2.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2nq2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2NQ2 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nq2 OCA], [https://pdbe.org/2nq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nq2 RCSB], [https://www.ebi.ac.uk/pdbsum/2nq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nq2 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/MOLB_HAEIN MOLB_HAEIN] Part of the ABC transporter complex MolBCA involved in molybdate import (PubMed:22078568, PubMed:24722984). Responsible for the translocation of the substrate across the membrane (PubMed:24722984). Functions as a low-affinity molybdate transporter (PubMed:24722984).<ref>PMID:22078568</ref> <ref>PMID:24722984</ref> | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nq/2nq2_consurf.spt"</scriptWhenChecked> | |
| - | == | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2nq2 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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 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<ref>PMID:17158291</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 2nq2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Lee | + | [[Category: Lee AT]] |
| - | [[Category: Locher | + | [[Category: Locher KP]] |
| - | [[Category: Lum | + | [[Category: Lum P]] |
| - | [[Category: Pinkett | + | [[Category: Pinkett HP]] |
| - | [[Category: Rees | + | [[Category: Rees DC]] |
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Current revision
An inward-facing conformation of a putative metal-chelate type ABC transporter.
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