2l55: Difference between revisions
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==Solution structure of the C-terminal domain of SilB from Cupriavidus metallidurans== | |||
<StructureSection load='2l55' size='340' side='right' caption='[[2l55]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2l55]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cupriavidus_metallidurans Cupriavidus metallidurans]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L55 FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rmet_6135, silB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119219 Cupriavidus metallidurans])</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=2l55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l55 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l55 RCSB], [http://www.ebi.ac.uk/pdbsum/2l55 PDBsum]</span></td></tr> | |||
</table> | |||
<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> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cupriavidus metallidurans]] | [[Category: Cupriavidus metallidurans]] | ||
[[Category: Bersch, B | [[Category: Bersch, B]] | ||
[[Category: Derfoufi, K | [[Category: Derfoufi, K]] | ||
[[Category: Vandenbussche, G | [[Category: Vandenbussche, G]] | ||
[[Category: Apo form]] | [[Category: Apo form]] | ||
[[Category: Cusf ortholog]] | [[Category: Cusf ortholog]] | ||
[[Category: Metal binding protein]] | [[Category: Metal binding protein]] | ||
