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4av3

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Crystal structure of Thermotoga Maritima sodium pumping membrane integral pyrophosphatase with metal ions in active site

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 ==Crystal structure of Thermotoga Maritima sodium pumping membrane integral pyrophosphatase with metal ions in active site==
-<StructureSection load='4av3' size='340' side='right' caption='[[4av3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='4av3' size='340' side='right'caption='[[4av3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4av3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AV3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AV3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4av3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AV3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AV3 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4av6|4av6]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] </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=4av3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4av3 OCA], [https://pdbe.org/4av3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4av3 RCSB], [https://www.ebi.ac.uk/pdbsum/4av3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4av3 ProSAT]</span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4av3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4av3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4av3 RCSB], [http://www.ebi.ac.uk/pdbsum/4av3 PDBsum]</span></td></tr>
+</table>
-<table>
+== Function ==
-<div style="background-color:#fffaf0;">
+[https://www.uniprot.org/uniprot/HPPA_THEMA HPPA_THEMA] Sodium pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for Na(+) movement across the membrane.[HAMAP-Rule:MF_01129]<ref>PMID:11343697</ref> <ref>PMID:17605473</ref> <ref>PMID:22837527</ref>
-== Publication Abstract from PubMed ==
-Membrane-integral pyrophosphatases (M-PPases) are crucial for the survival of plants, bacteria, and protozoan parasites. They couple pyrophosphate hydrolysis or synthesis to Na(+) or H(+) pumping. The 2.6-angstrom structure of Thermotoga maritima M-PPase in the resting state reveals a previously unknown solution for ion pumping. The hydrolytic center, 20 angstroms above the membrane, is coupled to the gate formed by the conserved Asp(243), Glu(246), and Lys(707) by an unusual "coupling funnel" of six alpha helices. Comparison with our 4.0-angstrom resolution structure of the product complex suggests that helix 12 slides down upon substrate binding to open the gate by a simple binding-change mechanism. Below the gate, four helices form the exit channel. Superimposing helices 3 to 6, 9 to 12, and 13 to 16 suggests that M-PPases arose through gene triplication.
-The structure and catalytic cycle of a sodium-pumping pyrophosphatase.,Kellosalo J, Kajander T, Kogan K, Pokharel K, Goldman A Science. 2012 Jul 27;337(6093):473-6. PMID:22837527<ref>PMID:22837527</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Inorganic diphosphatase]]
+[[Category: Large Structures]]
 [[Category: Thermotoga maritima]]
-[[Category: Goldman, A.]]
+[[Category: Goldman A]]
-[[Category: Kajander, T.]]
+[[Category: Kajander T]]
-[[Category: Kellosalo, J.]]
+[[Category: Kellosalo J]]
-[[Category: Kogan, K.]]
+[[Category: Kogan K]]
-[[Category: Pokharel, K.]]
+[[Category: Pokharel K]]
-[[Category: Hydrolase]]
-[[Category: Ion pump]]
-[[Category: Membrane pyrophosphotase]]

4av3

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Crystal structure of Thermotoga Maritima sodium pumping membrane integral pyrophosphatase with metal ions in active site

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