5nqm: Difference between revisions
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==CU(I)-CSP3 (COPPER STORAGE PROTEIN 3) FROM METHYLOSINUS== | |||
<StructureSection load='5nqm' size='340' side='right'caption='[[5nqm]], [[Resolution|resolution]] 1.59Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5nqm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylosinus_trichosporium_OB3b Methylosinus trichosporium OB3b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NQM FirstGlance]. <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]] 1.59Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=5nqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nqm OCA], [https://pdbe.org/5nqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nqm RCSB], [https://www.ebi.ac.uk/pdbsum/5nqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nqm ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1I9GEP2_METTR A0A1I9GEP2_METTR] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacteria possess cytosolic proteins (Csp3s) capable of binding large quantities of copper and preventing toxicity. Crystal structures of a Csp3 plus increasing amounts of CuI provide atomic-level information about how a storage protein loads with metal ions. Many more sites are occupied than CuI equiv added, with binding by twelve central sites dominating. These can form [Cu4 (S-Cys)4 ] intermediates leading to [Cu4 (S-Cys)5 ]- , [Cu4 (S-Cys)6 ]2- , and [Cu4 (S-Cys)5 (O-Asn)]- clusters. Construction of the five CuI sites at the opening of the bundle lags behind the main core, and the two least accessible sites at the opposite end of the bundle are occupied last. Facile CuI cluster formation, reminiscent of that for inorganic complexes with organothiolate ligands, is largely avoided in biology but is used by proteins that store copper in the cytosol of prokaryotes and eukaryotes, where this reactivity is also key to toxicity. | |||
Visualizing Biological Copper Storage: The Importance of Thiolate-Coordinated Tetranuclear Clusters.,Basle A, Platsaki S, Dennison C Angew Chem Int Ed Engl. 2017 Jul 17;56(30):8697-8700. doi:, 10.1002/anie.201703107. Epub 2017 Jun 19. PMID:28504850<ref>PMID:28504850</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5nqm" style="background-color:#fffaf0;"></div> | ||
[[Category: Dennison | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methylosinus trichosporium OB3b]] | |||
[[Category: Basle A]] | |||
[[Category: Dennison C]] | |||
[[Category: Platsaki S]] | |||
Latest revision as of 12:02, 22 November 2023
CU(I)-CSP3 (COPPER STORAGE PROTEIN 3) FROM METHYLOSINUS
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