2l55: Difference between revisions
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New page: '''Unreleased structure''' The entry 2l55 is ON HOLD Authors: Bersch, B., Derfoufi, K., Vandenbussche, G. Description: Solution structure of the C-terminal domain of SilB from Cupriavi... |
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The | ==Solution structure of the C-terminal domain of SilB from Cupriavidus metallidurans== | ||
<StructureSection load='2l55' size='340' side='right'caption='[[2l55]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2l55]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_metallidurans_CH34 Cupriavidus metallidurans CH34]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L55 FirstGlance]. <br> | |||
</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=2l55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l55 OCA], [https://pdbe.org/2l55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l55 RCSB], [https://www.ebi.ac.uk/pdbsum/2l55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l55 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q58AF3_CUPMC Q58AF3_CUPMC] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Detoxification of heavy metal ions in Proteobacteria is tightly controlled by various systems regulating their sequestration and transport. In Cupriavidus metallidurans CH34, a model organism for heavy metal resistance studies, the sil determinant is potentially involved in silver and copper ions efflux. Proteins SilA, SilB, and SilC form a Resistance Nodulation cell Division (RND)-based transport system where SilB is the periplasmic adaptor protein belonging to the Membrane Fusion Protein (MFP) family. In addition to the four domains typical of known MFPs, SilB has a fifth additional C-terminal domain, called SilB440-521, which is characterized here. Structure and backbone dynamics of SilB440-521 have been investigated using NMR and the residues of the metal site were identified from 15N and 13C-edited HSQC spectra. The solution structure and additional metal binding experiments demonstrated that this C-terminal domain folds independently of the rest of the protein and has a conformation and a Ag+ and Cu+ binding specificity similar to those determined for CusF from Escherichia coli. The small protein CusF plays a role in metal-trafficking in the periplasm. The similarity with CusF suggests a potential metallochaperone role for SilB440-521 that is discussed in the context of simultaneous expression of different determinants involved in copper resistance in C. metallidurans CH34. | |||
Structural and metal-binding characterization of the C-terminal metallochaperone domain of the membrane fusion protein SilB from Cupriavidus metallidurans CH34.,Bersch B, Derfoufi KM, De Angelis F, Auquier V, Ngolong Ekende E, Mergeay M, Ruysschaert JM, Vandenbussche G Biochemistry. 2011 Feb 7. PMID:21299248<ref>PMID:21299248</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2l55" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cupriavidus metallidurans CH34]] | |||
[[Category: Large Structures]] | |||
[[Category: Bersch B]] | |||
[[Category: Derfoufi K]] | |||
[[Category: Vandenbussche G]] | |||
Latest revision as of 05:39, 15 May 2024
Solution structure of the C-terminal domain of SilB from Cupriavidus metallidurans
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