1mhs: Difference between revisions
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<StructureSection load='1mhs' size='340' side='right'caption='[[1mhs]], [[Resolution|resolution]] 8.00Å' scene=''> | <StructureSection load='1mhs' size='340' side='right'caption='[[1mhs]], [[Resolution|resolution]] 8.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mhs]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1mhs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MHS FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eul|1eul]], [[1iwo|1iwo]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eul|1eul]], [[1iwo|1iwo]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Proton-exporting_ATPase Proton-exporting ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.6 3.6.3.6] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhs OCA], [https://pdbe.org/1mhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mhs RCSB], [https://www.ebi.ac.uk/pdbsum/1mhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mhs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/PMA1_NEUCR PMA1_NEUCR]] The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 10:24, 27 January 2022
Model of Neurospora crassa proton ATPaseModel of Neurospora crassa proton ATPase
Structural highlights
Function[PMA1_NEUCR] The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProton pumps in the plasma membrane of plants and yeasts maintain the intracellular pH and membrane potential. To gain insight into the molecular mechanisms of proton pumping, we built an atomic homology model of the proton pump based on the 2.6 angstrom x-ray structure of the related Ca2+ pump from rabbit sarcoplasmic reticulum. The model, when fitted to an 8 angstrom map of the Neurospora proton pump determined by electron microscopy, reveals the likely path of the proton through the membrane and shows that the nucleotide-binding domain rotates by approximately 70 degrees to deliver adenosine triphosphate (ATP) to the phosphorylation site. A synthetic peptide corresponding to the carboxyl-terminal regulatory domain stimulates ATPase activity, suggesting a mechanism for proton transport regulation. Structure, mechanism, and regulation of the Neurospora plasma membrane H+-ATPase.,Kuhlbrandt W, Zeelen J, Dietrich J Science. 2002 Sep 6;297(5587):1692-6. Epub 2002 Aug 8. PMID:12169656[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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