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3k6x
From Proteopedia
(Difference between revisions)
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==M. acetivorans Molybdate-Binding Protein (ModA) in Molybdate-Bound Close Form with 2 Molecules in Asymmetric Unit Forming Beta Barrel== | ==M. acetivorans Molybdate-Binding Protein (ModA) in Molybdate-Bound Close Form with 2 Molecules in Asymmetric Unit Forming Beta Barrel== | ||
| - | <StructureSection load='3k6x' size='340' side='right' caption='[[3k6x]], [[Resolution|resolution]] 2.25Å' scene=''> | + | <StructureSection load='3k6x' size='340' side='right'caption='[[3k6x]], [[Resolution|resolution]] 2.25Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3k6x]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3k6x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans Methanosarcina acetivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K6X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K6X FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MOO:MOLYBDATE+ION'>MOO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3k6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k6x OCA], [https://pdbe.org/3k6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k6x RCSB], [https://www.ebi.ac.uk/pdbsum/3k6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k6x ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Y280_METAC Y280_METAC] | ||
== 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/k6/3k6x_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k6/3k6x_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> | ||
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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=3k6x ConSurf]. | </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=3k6x ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The trace-element oxyanion molybdate, which is required for the growth of many bacterial and archaeal species, is transported into the cell by an ATP-binding cassette (ABC) transporter superfamily uptake system called ModABC. ModABC consists of the ModA periplasmic solute-binding protein, the integral membrane-transport protein ModB and the ATP-binding and hydrolysis cassette protein ModC. In this study, X-ray crystal structures of ModA from the archaeon Methanosarcina acetivorans (MaModA) have been determined in the apoprotein conformation at 1.95 and 1.69 A resolution and in the molybdate-bound conformation at 2.25 and 2.45 A resolution. The overall domain structure of MaModA is similar to other ModA proteins in that it has a bilobal structure in which two mixed alpha/beta domains are linked by a hinge region. The apo MaModA is the first unliganded archaeal ModA structure to be determined: it exhibits a deep cleft between the two domains and confirms that upon binding ligand one domain is rotated towards the other by a hinge-bending motion, which is consistent with the 'Venus flytrap' model seen for bacterial-type periplasmic binding proteins. In contrast to the bacterial ModA structures, which have tetrahedral coordination of their metal substrates, molybdate-bound MaModA employs octahedral coordination of its substrate like other archaeal ModA proteins. | ||
| - | + | ==See Also== | |
| - | + | *[[ABC transporter 3D structures|ABC transporter 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Arbing | + | [[Category: Methanosarcina acetivorans]] |
| - | [[Category: Chan | + | [[Category: Arbing MA]] |
| - | [[Category: Chernishof | + | [[Category: Chan S]] |
| - | [[Category: Chiang | + | [[Category: Chernishof I]] |
| - | [[Category: Giuroiu | + | [[Category: Chiang J]] |
| - | [[Category: Gunsalus | + | [[Category: Giuroiu I]] |
| - | [[Category: Perry | + | [[Category: Gunsalus RP]] |
| - | [[Category: Sawaya | + | [[Category: Perry LJ]] |
| - | + | [[Category: Sawaya MR]] | |
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Current revision
M. acetivorans Molybdate-Binding Protein (ModA) in Molybdate-Bound Close Form with 2 Molecules in Asymmetric Unit Forming Beta Barrel
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