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| | ==The crystal structure of a Cu(I) metallochaperone from Streptomyces lividans== | | ==The crystal structure of a Cu(I) metallochaperone from Streptomyces lividans== |
| - | <StructureSection load='3zja' size='340' side='right' caption='[[3zja]], [[Resolution|resolution]] 1.48Å' scene=''> | + | <StructureSection load='3zja' size='340' side='right'caption='[[3zja]], [[Resolution|resolution]] 1.48Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zja]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZJA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZJA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zja]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZJA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> |
| - | <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=3zja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zja OCA], [http://pdbe.org/3zja PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zja RCSB], [http://www.ebi.ac.uk/pdbsum/3zja PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zja ProSAT]</span></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=3zja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zja OCA], [https://pdbe.org/3zja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zja RCSB], [https://www.ebi.ac.uk/pdbsum/3zja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zja ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Actinomyces lividans krasil'nikov et al. 1965]] | | [[Category: Actinomyces lividans krasil'nikov et al. 1965]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Blundell, K L.I M]] | | [[Category: Blundell, K L.I M]] |
| | [[Category: Hough, M]] | | [[Category: Hough, M]] |
| | [[Category: Worrall, J A.R]] | | [[Category: Worrall, J A.R]] |
| | [[Category: Chaperone]] | | [[Category: Chaperone]] |
| Structural highlights
Publication Abstract from PubMed
In Streptomyces lividans an extracytoplasmic copper-binding Sco protein plays a role in two unlinked processes: (i) initiating a morphological development switch and (ii) facilitating the co-factoring of the CuA domain of CcO (cytochrome c oxidase). How Sco obtains copper once secreted to the extracytoplasmic environment is unknown. In the present paper we report on a protein possessing an HX6MX21HXM motif that binds a single cuprous ion with subfemtomolar affinity. High-resolution X-ray structures of this extracytoplasmic copper chaperone-like protein (ECuC) in the apo- and Cu(I)-bound states reveal that the latter possesses a surface-accessible cuprous-ion-binding site located in a dish-shaped region of beta-sheet structure. A cuprous ion is transferred under a favourable thermodynamic gradient from ECuC to Sco with no back transfer occurring. The ionization properties of the cysteine residues in the Cys86xxxCys90 copper-binding motif of Sco, together with their positional locations identified from an X-ray structure of Sco, suggests a role for Cys86 in initiating an inter-complex ligand-exchange reaction with Cu(I)-ECuC. Generation of the genetic knockouts, Deltasco, Deltaecuc and Deltasco/ecuc, and subsequent in vivo assays lend support to the existence of a branched extracytoplasmic copper-trafficking pathway in S. lividans. One branch requires both Sco and to a certain extent ECuC to cofactor the CuA domain, whereas the other uses only Sco to deliver copper to a cuproenzyme to initiate morphological development.
Structural and mechanistic insights into an extracytoplasmic copper trafficking pathway in Streptomyces lividans.,Blundell KL, Hough MA, Vijgenboom E, Worrall JA Biochem J. 2014 May 1;459(3):525-38. doi: 10.1042/BJ20140017. PMID:24548299[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Blundell KL, Hough MA, Vijgenboom E, Worrall JA. Structural and mechanistic insights into an extracytoplasmic copper trafficking pathway in Streptomyces lividans. Biochem J. 2014 May 1;459(3):525-38. doi: 10.1042/BJ20140017. PMID:24548299 doi:http://dx.doi.org/10.1042/BJ20140017
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