|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==An inward-facing conformation of a putative metal-chelate type ABC transporter.== | | ==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=''> | + | <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/"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> | + | <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='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> | + | </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'>[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> | + | <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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Y1471_HAEIN Y1471_HAEIN]] Probably part of a binding-protein-dependent transport system. Probably responsible for the translocation of the substrate across the membrane. | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nq/2nq2_consurf.spt"</scriptWhenChecked> | + | <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> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| Line 31: |
Line 32: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium influenzae lehmann and neumann 1896]] | + | [[Category: Haemophilus influenzae]] |
| - | [[Category: Lee, A T]] | + | [[Category: Large Structures]] |
| - | [[Category: Locher, K P]] | + | [[Category: Lee AT]] |
| - | [[Category: Lum, P]] | + | [[Category: Locher KP]] |
| - | [[Category: Pinkett, H P]] | + | [[Category: Lum P]] |
| - | [[Category: Rees, D C]] | + | [[Category: Pinkett HP]] |
| - | [[Category: Atp-binding protein]] | + | [[Category: Rees DC]] |
| - | [[Category: Metal transport]]
| + | |
| - | [[Category: Nucleotide binding domain]]
| + | |
| - | [[Category: Putative iron chelatin abc transporter]]
| + | |
| - | [[Category: Transmembrane domain]]
| + | |
| Structural highlights
Function
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).[1] [2]
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 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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tirado-Lee L, Lee A, Rees DC, Pinkett HW. Classification of a Haemophilus influenzae ABC Transporter HI1470/71 through Its Cognate Molybdate Periplasmic Binding Protein, MolA. Structure. 2011 Nov 9;19(11):1701-10. PMID:22078568 doi:10.1016/j.str.2011.10.004
- ↑ Rice AJ, Harrison A, Alvarez FJ, Davidson AL, Pinkett HW. Small substrate transport and mechanism of a molybdate ATP binding cassette transporter in a lipid environment. J Biol Chem. 2014 May 23;289(21):15005-13. PMID:24722984 doi:10.1074/jbc.M114.563783
- ↑ Pinkett HW, Lee AT, Lum P, Locher KP, Rees DC. An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science. 2007 Jan 19;315(5810):373-7. Epub 2006 Dec 7. PMID:17158291
|
