4bbj: Difference between revisions

Latest revision as of 10:40, 6 November 2024

Copper-transporting PIB-ATPase in complex with beryllium fluoride representing the E2P state

Structural highlights

4bbj is a 1 chain structure with sequence from Legionella pneumophila subsp. pneumophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.75Å
Ligands:	BFD, CE1, MG, NAD, PC
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

COPA_LEGPH Couples the hydrolysis of ATP with the export of copper.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Heavy metals in cells are typically regulated by PIB-type ATPases. The first structure of the class, a Cu+-ATPase from Legionella pneumophila (LpCopA), outlined a copper transport pathway across the membrane, which was inferred to be occluded. Here we show by molecular dynamics simulations that extracellular water solvated the transmembrane (TM) domain, results indicative of a Cu+-release pathway. Furthermore, a new LpCopA crystal structure determined at 2.8-A resolution, trapped in the preceding E2P state, delineated the same passage, and site-directed-mutagenesis activity assays support a functional role for the conduit. The structural similarities between the TM domains of the two conformations suggest that Cu+-ATPases couple dephosphorylation and ion extrusion differently than do the well-characterized PII-type ATPases. The ion pathway explains why certain Menkes' and Wilson's disease mutations impair protein function and points to a site for inhibitors targeting pathogens.

Copper-transporting P-type ATPases use a unique ion-release pathway.,Andersson M, Mattle D, Sitsel O, Klymchuk T, Nielsen AM, Moller LB, White SH, Nissen P, Gourdon P Nat Struct Mol Biol. 2013 Dec 8. doi: 10.1038/nsmb.2721. PMID:24317491^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Andersson M, Mattle D, Sitsel O, Klymchuk T, Nielsen AM, Moller LB, White SH, Nissen P, Gourdon P. Copper-transporting P-type ATPases use a unique ion-release pathway. Nat Struct Mol Biol. 2013 Dec 8. doi: 10.1038/nsmb.2721. PMID:24317491 doi:https://dx.doi.org/10.1038/nsmb.2721
↑ Placenti MA, Roman EA, González Flecha FL, González-Lebrero RM. Functional characterization of Legionella pneumophila Cu(+) transport ATPase. The activation by Cu(+) and ATP. Biochim Biophys Acta Biomembr. 2022 Feb 1;1864(2):183822. PMID:34826402 doi:10.1016/j.bbamem.2021.183822
↑ Gourdon P, Liu XY, Skjorringe T, Morth JP, Moller LB, Pedersen BP, Nissen P. Crystal structure of a copper-transporting PIB-type ATPase. Nature. 2011 Jun 29;475(7354):59-64. doi: 10.1038/nature10191. PMID:21716286 doi:10.1038/nature10191
↑ Andersson M, Mattle D, Sitsel O, Klymchuk T, Nielsen AM, Moller LB, White SH, Nissen P, Gourdon P. Copper-transporting P-type ATPases use a unique ion-release pathway. Nat Struct Mol Biol. 2013 Dec 8. doi: 10.1038/nsmb.2721. PMID:24317491 doi:https://dx.doi.org/10.1038/nsmb.2721

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Andersson M, Mattle D, Sitsel O, Klymchuk T, Nielsen AM, Moller LB, White SH, Nissen P, Gourdon P. Copper-transporting P-type ATPases use a unique ion-release pathway. Nat Struct Mol Biol. 2013 Dec 8. doi: 10.1038/nsmb.2721. PMID:24317491 doi:https://dx.doi.org/10.1038/nsmb.2721

[2] Placenti MA, Roman EA, González Flecha FL, González-Lebrero RM. Functional characterization of Legionella pneumophila Cu(+) transport ATPase. The activation by Cu(+) and ATP. Biochim Biophys Acta Biomembr. 2022 Feb 1;1864(2):183822. PMID:34826402 doi:10.1016/j.bbamem.2021.183822

[3] Gourdon P, Liu XY, Skjorringe T, Morth JP, Moller LB, Pedersen BP, Nissen P. Crystal structure of a copper-transporting PIB-type ATPase. Nature. 2011 Jun 29;475(7354):59-64. doi: 10.1038/nature10191. PMID:21716286 doi:10.1038/nature10191

[4] Andersson M, Mattle D, Sitsel O, Klymchuk T, Nielsen AM, Moller LB, White SH, Nissen P, Gourdon P. Copper-transporting P-type ATPases use a unique ion-release pathway. Nat Struct Mol Biol. 2013 Dec 8. doi: 10.1038/nsmb.2721. PMID:24317491 doi:https://dx.doi.org/10.1038/nsmb.2721

[1]

[2]

[3]

[4]

@@ Line 1: / Line 1: @@
-{{STRUCTURE_4bbj|  PDB=4bbj  |  SCENE=  }}
-===ATPase crystal structure===
-==About this Structure==
+==Copper-transporting PIB-ATPase in complex with beryllium fluoride representing the E2P state==
-[[4bbj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BBJ OCA].
+<StructureSection load='4bbj' size='340' side='right'caption='[[4bbj]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
-[[Category: Gourdon, P.]]
+== Structural highlights ==
-[[Category: Mattle, D.]]
+<table><tr><td colspan='2'>[[4bbj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila Legionella pneumophila subsp. pneumophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BBJ FirstGlance]. <br>
-[[Category: Nissen, P.]]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
-[[Category: Cation transport protein]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=CE1:O-DODECANYL+OCTAETHYLENE+GLYCOL'>CE1</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PC:PHOSPHOCHOLINE'>PC</scene></td></tr>
-[[Category: Cell membrane]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bbj OCA], [https://pdbe.org/4bbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bbj RCSB], [https://www.ebi.ac.uk/pdbsum/4bbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bbj ProSAT]</span></td></tr>
-[[Category: Hepatolenticular degeneration]]
+</table>
-[[Category: Hydrolase]]
+== Function ==
-[[Category: Membrane protein]]
+[https://www.uniprot.org/uniprot/COPA_LEGPH COPA_LEGPH] Couples the hydrolysis of ATP with the export of copper.<ref>PMID:24317491</ref> <ref>PMID:34826402</ref> <ref>PMID:21716286</ref>
-[[Category: Menkes disease]]
+<div style="background-color:#fffaf0;">
-[[Category: Sarcoplasmic reticulum calcium-transporting atpase]]
+== Publication Abstract from PubMed ==
-[[Category: Structure-activity relationship]]
+Heavy metals in cells are typically regulated by PIB-type ATPases. The first structure of the class, a Cu+-ATPase from Legionella pneumophila (LpCopA), outlined a copper transport pathway across the membrane, which was inferred to be occluded. Here we show by molecular dynamics simulations that extracellular water solvated the transmembrane (TM) domain, results indicative of a Cu+-release pathway. Furthermore, a new LpCopA crystal structure determined at 2.8-A resolution, trapped in the preceding E2P state, delineated the same passage, and site-directed-mutagenesis activity assays support a functional role for the conduit. The structural similarities between the TM domains of the two conformations suggest that Cu+-ATPases couple dephosphorylation and ion extrusion differently than do the well-characterized PII-type ATPases. The ion pathway explains why certain Menkes' and Wilson's disease mutations impair protein function and points to a site for inhibitors targeting pathogens.
-[[Category: Wilson disease]]
+Copper-transporting P-type ATPases use a unique ion-release pathway.,Andersson M, Mattle D, Sitsel O, Klymchuk T, Nielsen AM, Moller LB, White SH, Nissen P, Gourdon P Nat Struct Mol Biol. 2013 Dec 8. doi: 10.1038/nsmb.2721. PMID:24317491<ref>PMID:24317491</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4bbj" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[ATPase 3D structures|ATPase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Legionella pneumophila subsp. pneumophila]]
+[[Category: Gourdon P]]
+[[Category: Mattle D]]
+[[Category: Nissen P]]

4bbj: Difference between revisions

Latest revision as of 10:40, 6 November 2024

Copper-transporting PIB-ATPase in complex with beryllium fluoride representing the E2P state

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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