2l55: Difference between revisions

<StructureSection load='2l55' size='340' side='right'caption='[[2l55]]' scene=''>

<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>

<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>

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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

</StructureSection>

[[Category: Cupriavidus metallidurans CH34]]

[[Category: Large Structures]]

[[Category: Bersch B]]

[[Category: Derfoufi K]]

[[Category: Vandenbussche G]]