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1on4

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Current revision

Solution structure of soluble domain of Sco1 from Bacillus Subtilis

Structural highlights

1on4 is a 1 chain structure with sequence from Bacillus subtilis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SCO1_BACSU Neccessary for insertion of copper into the active site of cytochrome c oxidase. May play a role in copper homeostasis or redox signaling.^[1] ^[2]

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 PubMed

Sco1, a protein required for the proper assembly of cytochrome c oxidase, has a soluble domain anchored to the cytoplasmic membrane through a single transmembrane segment. The solution structure of the soluble part of apoSco1 from Bacillus subtilis has been solved by NMR and the internal mobility characterized. Its fold places Sco1 in a distinct subgroup of the functionally unrelated thioredoxin proteins. In vitro Sco1 binds copper(I) through a CXXXCP motif and possibly His 135 and copper(II) in two different species, thus suggesting that copper(II) is adventitious more than physiological. The Sco1 structure represents the first structure of this class of proteins, present in a variety of eukaryotic and bacterial organisms, and elucidates a link between copper trafficking proteins and thioredoxins. The availability of the structure has allowed us to model the homologs Sco1 and Sco2 from S. cerevisiae and to discuss the physiological role of the Sco family.

Solution structure of Sco1: a thioredoxin-like protein Involved in cytochrome c oxidase assembly.,Balatri E, Banci L, Bertini I, Cantini F, Ciofi-Baffoni S Structure. 2003 Nov;11(11):1431-43. PMID:14604533^[3]

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

References

↑ Mattatall NR, Jazairi J, Hill BC. Characterization of YpmQ, an accessory protein required for the expression of cytochrome c oxidase in Bacillus subtilis. J Biol Chem. 2000 Sep 15;275(37):28802-9. PMID:10837475 doi:http://dx.doi.org/10.1074/jbc.M002741200
↑ Ye Q, Imriskova-Sosova I, Hill BC, Jia Z. Identification of a disulfide switch in BsSco, a member of the Sco family of cytochrome c oxidase assembly proteins. Biochemistry. 2005 Mar 1;44(8):2934-42. PMID:15723536 doi:10.1021/bi0480537
↑ Balatri E, Banci L, Bertini I, Cantini F, Ciofi-Baffoni S. Solution structure of Sco1: a thioredoxin-like protein Involved in cytochrome c oxidase assembly. Structure. 2003 Nov;11(11):1431-43. PMID:14604533

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1on4"

@@ Line 1: / Line 1: @@
 ==Solution structure of soluble domain of Sco1 from Bacillus Subtilis==
-<StructureSection load='1on4' size='340' side='right'caption='[[1on4]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
+<StructureSection load='1on4' size='340' side='right'caption='[[1on4]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1on4]] 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=1ON4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ON4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1on4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ON4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ON4 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YPMQ ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1on4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1on4 OCA], [https://pdbe.org/1on4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1on4 RCSB], [https://www.ebi.ac.uk/pdbsum/1on4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1on4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/SCO1_BACSU SCO1_BACSU]] Neccessary for insertion of copper into the active site of cytochrome c oxidase. May play a role in copper homeostasis or redox signaling.<ref>PMID:10837475</ref> <ref>PMID:15723536</ref>
+[https://www.uniprot.org/uniprot/SCO1_BACSU SCO1_BACSU] Neccessary for insertion of copper into the active site of cytochrome c oxidase. May play a role in copper homeostasis or redox signaling.<ref>PMID:10837475</ref> <ref>PMID:15723536</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Vibrio subtilis ehrenberg 1835]]
+[[Category: Bacillus subtilis]]
 [[Category: Large Structures]]
-[[Category: Balatri, E]]
+[[Category: Balatri E]]
-[[Category: Banci, L]]
+[[Category: Banci L]]
-[[Category: Bertini, I]]
+[[Category: Bertini I]]
-[[Category: Cantini, F]]
+[[Category: Cantini F]]
-[[Category: Ciofi-Baffoni, S]]
+[[Category: Ciofi-Baffoni S]]
-[[Category: SPINE, Structural Proteomics in Europe]]
-[[Category: Copper protein]]
-[[Category: Cox assembly protein]]
-[[Category: Metal binding protein]]
-[[Category: Sco1 from b. subtili]]
-[[Category: Spine]]
-[[Category: Structural genomic]]
-[[Category: Structural proteomics in europe]]
-[[Category: Thioredoxin-like fold]]
-[[Category: Ypmq]]

1on4

From Proteopedia

Current revision

Solution structure of soluble domain of Sco1 from Bacillus Subtilis

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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