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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]] 2.25&Aring;' scene=''>
<StructureSection load='3k6x' size='340' side='right'caption='[[3k6x]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3k6x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35395 Atcc 35395]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K6X FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MOO:MOLYBDATE+ION'>MOO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.25&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3k6u|3k6u]], [[3k6v|3k6v]], [[3k6w|3k6w]]</td></tr>
<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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MA0280, MA_0280 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2214 ATCC 35395])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3k6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k6x OCA], [http://pdbe.org/3k6x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k6x RCSB], [http://www.ebi.ac.uk/pdbsum/3k6x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k6x ProSAT]</span></td></tr>
</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>
Line 19: Line 20:
</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.


Apo and ligand-bound structures of ModA from the archaeon Methanosarcina acetivorans.,Chan S, Giuroiu I, Chernishof I, Sawaya MR, Chiang J, Gunsalus RP, Arbing MA, Perry LJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Mar 1;66(Pt, 3):242-50. Epub 2010 Feb 23. PMID:20208152<ref>PMID:20208152</ref>
==See Also==
 
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3k6x" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 35395]]
[[Category: Large Structures]]
[[Category: Arbing, M A]]
[[Category: Methanosarcina acetivorans]]
[[Category: Chan, S]]
[[Category: Arbing MA]]
[[Category: Chernishof, I]]
[[Category: Chan S]]
[[Category: Chiang, J]]
[[Category: Chernishof I]]
[[Category: Giuroiu, I]]
[[Category: Chiang J]]
[[Category: Gunsalus, R P]]
[[Category: Giuroiu I]]
[[Category: Perry, L J]]
[[Category: Gunsalus RP]]
[[Category: Sawaya, M R]]
[[Category: Perry LJ]]
[[Category: Abc transporter]]
[[Category: Sawaya MR]]
[[Category: Ligand]]
[[Category: Metal-binding protein]]
[[Category: Methanosarcina acetivoran]]
[[Category: Moda]]
[[Category: Molybdate]]
[[Category: Periplasmic binding protein]]
[[Category: Transport protein]]

Latest revision as of 13:15, 21 February 2024

M. acetivorans Molybdate-Binding Protein (ModA) in Molybdate-Bound Close Form with 2 Molecules in Asymmetric Unit Forming Beta BarrelM. acetivorans Molybdate-Binding Protein (ModA) in Molybdate-Bound Close Form with 2 Molecules in Asymmetric Unit Forming Beta Barrel

Structural highlights

3k6x is a 2 chain structure with sequence from Methanosarcina acetivorans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Y280_METAC

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3k6x, resolution 2.25Å

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OCA
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