4av6

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<StructureSection load='4av6' size='340' side='right'caption='[[4av6]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
<StructureSection load='4av6' size='340' side='right'caption='[[4av6]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4av6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AV6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AV6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4av6]] 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=4AV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AV6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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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]] 4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4av3|4av3]]</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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='activity'><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>
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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=4av6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4av6 OCA], [https://pdbe.org/4av6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4av6 RCSB], [https://www.ebi.ac.uk/pdbsum/4av6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4av6 ProSAT]</span></td></tr>
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<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=4av6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4av6 OCA], [http://pdbe.org/4av6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4av6 RCSB], [http://www.ebi.ac.uk/pdbsum/4av6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4av6 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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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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<div class="pdbe-citations 4av6" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43589]]
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[[Category: Large Structures]]
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[[Category: Inorganic diphosphatase]]
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[[Category: Thermotoga maritima]]
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[[Category: Goldman, A]]
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[[Category: Goldman A]]
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[[Category: Kajander, T]]
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[[Category: Kajander T]]
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[[Category: Kellosalo, J]]
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[[Category: Kellosalo J]]
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[[Category: Kogan, K]]
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[[Category: Kogan K]]
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[[Category: Pokharel, K]]
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[[Category: Pokharel K]]
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[[Category: Hydrolase]]
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[[Category: Membrane protein]]
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[[Category: Sodium pump]]
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Current revision

Crystal structure of Thermotoga maritima sodium pumping membrane integral pyrophosphatase at 4 A in complex with phosphate and magnesium

PDB ID 4av6

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