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2nq2

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{{Seed}}
 
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[[Image:2nq2.png|left|200px]]
 
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==An inward-facing conformation of a putative metal-chelate type ABC transporter.==
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The line below this paragraph, containing "STRUCTURE_2nq2", creates the "Structure Box" on the page.
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<StructureSection load='2nq2' size='340' side='right'caption='[[2nq2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<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>
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{{STRUCTURE_2nq2| PDB=2nq2 | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nq/2nq2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===An inward-facing conformation of a putative metal-chelate type ABC transporter.===
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17158291}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2nq2" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17158291 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17158291}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2NQ2 is a 4 chains structure of sequences from [http://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].
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==Reference==
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<ref group="xtra">PMID:17158291</ref><references group="xtra"/>
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[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
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[[Category: Lee, A T.]]
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[[Category: Large Structures]]
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[[Category: Locher, K P.]]
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[[Category: Lee AT]]
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[[Category: Lum, P.]]
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[[Category: Locher KP]]
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[[Category: Pinkett, H P.]]
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[[Category: Lum P]]
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[[Category: Rees, D C.]]
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[[Category: Pinkett HP]]
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[[Category: Atp-binding protein]]
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[[Category: Rees DC]]
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[[Category: Nucleotide binding domain]]
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[[Category: Putative iron chelatin abc transporter]]
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[[Category: Transmembrane domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:40:58 2009''
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Current revision

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

PDB ID 2nq2

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