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2x79

From Proteopedia

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{{Seed}}
 
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[[Image:2x79.jpg|left|200px]]
 
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==Inward facing conformation of Mhp1==
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The line below this paragraph, containing "STRUCTURE_2x79", creates the "Structure Box" on the page.
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<StructureSection load='2x79' size='340' side='right'caption='[[2x79]], [[Resolution|resolution]] 3.80&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'>[[2x79]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Microbacterium_liquefaciens Microbacterium liquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X79 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]] 3.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_2x79| PDB=2x79 | SCENE= }}
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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=2x79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x79 OCA], [https://pdbe.org/2x79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x79 RCSB], [https://www.ebi.ac.uk/pdbsum/2x79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x79 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HYUP_MICLQ HYUP_MICLQ] Nucleobase-proton symporter that mediates the sodium-dependent binding and uptake of 5-aryl-substituted hydantoin compounds (PubMed:16621827, PubMed:24952894). 5-indolyl methyl hydantoin and 5-benzyl hydantoin are the preferred substrates, with selectivity for a hydrophobic substituent in position 5 of hydantoin and for the L isomer over the D isomer (PubMed:16621827, PubMed:24952894).<ref>PMID:16621827</ref> <ref>PMID:24952894</ref> <ref>PMID:16116274</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/x7/2x79_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=2x79 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 structure of the sodium-benzylhydantoin transport protein Mhp1 from Microbacterium liquefaciens comprises a five-helix inverted repeat, which is widespread among secondary transporters. Here, we report the crystal structure of an inward-facing conformation of Mhp1 at 3.8 angstroms resolution, complementing its previously described structures in outward-facing and occluded states. From analyses of the three structures and molecular dynamics simulations, we propose a mechanism for the transport cycle in Mhp1. Switching from the outward- to the inward-facing state, to effect the inward release of sodium and benzylhydantoin, is primarily achieved by a rigid body movement of transmembrane helices 3, 4, 8, and 9 relative to the rest of the protein. This forms the basis of an alternating access mechanism applicable to many transporters of this emerging superfamily.
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===INWARD FACING CONFORMATION OF MHP1===
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Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1.,Shimamura T, Weyand S, Beckstein O, Rutherford NG, Hadden JM, Sharples D, Sansom MS, Iwata S, Henderson PJ, Cameron AD Science. 2010 Apr 23;328(5977):470-3. PMID:20413494<ref>PMID:20413494</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_20413494}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2x79" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20413494 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20413494}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2X79 is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Microbacterium_liquefaciens Microbacterium liquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X79 OCA].
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==Reference==
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<ref group="xtra">PMID:20413494</ref><references group="xtra"/>
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[[Category: Microbacterium liquefaciens]]
[[Category: Microbacterium liquefaciens]]
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[[Category: Beckstein, O.]]
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[[Category: Beckstein O]]
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[[Category: Cameron, A D.]]
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[[Category: Cameron AD]]
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[[Category: Hadden, J M.]]
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[[Category: Hadden JM]]
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[[Category: Henderson, P J.F.]]
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[[Category: Henderson PJF]]
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[[Category: Iwata, S.]]
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[[Category: Iwata S]]
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[[Category: Rutherford, N G.]]
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[[Category: Rutherford NG]]
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[[Category: Sansom, M S.P.]]
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[[Category: Sansom MSP]]
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[[Category: Sharples, D.]]
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[[Category: Sharples D]]
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[[Category: Shimamura, T.]]
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[[Category: Shimamura T]]
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[[Category: Weyand, S.]]
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[[Category: Weyand S]]
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[[Category: Membrane protein]]
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[[Category: Transport protein]]
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[[Category: Transporter]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 5 11:51:01 2010''
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Current revision

Inward facing conformation of Mhp1

PDB ID 2x79

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