1p6t: Difference between revisions
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<StructureSection load='1p6t' size='340' side='right'caption='[[1p6t]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | <StructureSection load='1p6t' size='340' side='right'caption='[[1p6t]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1p6t]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1p6t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P6T FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1oq3|1oq3]], [[1kqk|1kqk]]</div></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;'>[[1oq3|1oq3]], [[1kqk|1kqk]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YVGX ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YVGX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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/Copper-exporting_ATPase Copper-exporting ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.4 3.6.3.4] </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=1p6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p6t OCA], [https://pdbe.org/1p6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p6t RCSB], [https://www.ebi.ac.uk/pdbsum/1p6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p6t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/COPA_BACSU COPA_BACSU]] Involved in copper export.<ref>PMID:12644235</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 18:12, 27 October 2021
Structure characterization of the water soluble region of P-type ATPase CopA from Bacillus subtilisStructure characterization of the water soluble region of P-type ATPase CopA from Bacillus subtilis
Structural highlights
Function[COPA_BACSU] Involved in copper export.[1] 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 PubMedThe solution structure of the N-terminal region (151 amino acids) of a copper ATPase, CopA, from Bacillus subtilis, is reported here. It consists of two domains, CopAa and CopAb, linked by two amino acids. It is found that the two domains, which had already been separately characterized, interact one to the other through a hydrogen bond network and a few hydrophobic interactions, forming a single rigid body. The two metal binding sites are far from one another, and the short link between the domains prevents them from interacting. This and the surface electrostatic potential suggest that each domain receives copper from the copper chaperone, CopZ, independently and transfers it to the membrane binding site of CopA. The affinity constants of silver(I) and copper(I) are similar for the two sites as monitored by NMR. Because the present construct "domain-short link-domain" is shared also by the last two domains of the eukaryotic copper ATPases and several residues at the interface between the two domains are conserved, the conclusions of the present study have general validity for the understanding of the function of copper ATPases. Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilis.,Banci L, Bertini I, Ciofi-Baffoni S, Gonnelli L, Su XC J Biol Chem. 2003 Dec 12;278(50):50506-13. Epub 2003 Sep 27. PMID:14514665[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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