6g64
From Proteopedia
(Difference between revisions)
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==MamM CTD H264A-E289A== | ==MamM CTD H264A-E289A== | ||
| - | <StructureSection load='6g64' size='340' side='right' caption='[[6g64]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='6g64' size='340' side='right'caption='[[6g64]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6g64]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G64 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G64 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6g64]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_6361 Dsm 6361]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G64 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G64 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mamM, mgI491, MGR_4095 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=55518 DSM 6361])</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=6g64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g64 OCA], [http://pdbe.org/6g64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g64 RCSB], [http://www.ebi.ac.uk/pdbsum/6g64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g64 ProSAT]</span></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=6g64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g64 OCA], [http://pdbe.org/6g64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g64 RCSB], [http://www.ebi.ac.uk/pdbsum/6g64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g64 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cation diffusion facilitator (CDF) proteins are a conserved family of transmembrane transporters that ensure cellular homeostasis of divalent transition metal cations. Metal cations bind to CDF protein's cytoplasmic C-terminal domain (CTD), leading to closure from its apo open V-shaped dimer to a tighter packed structure, followed by a conformational change of the transmembrane domain, thus enabling transport of the metal cation. By implementing a comprehensive range of biochemical and biophysical methods, we studied the molecular mechanism of metal binding to the magnetotactic bacterial CDF protein MamM CTD. Our results reveal that the CTD is rather dynamic in its apo form, and that two dependent metal-binding sites, a single central binding site and two symmetrical, peripheral sites, are available for metal binding. However, only cation binding to the peripheral sites leads to conformational changes that lock the protein in a compact state. Thus, this work reveals how metal binding is regulating the sequential uptakes of metal cations by MamM, and extends our understanding of the complex regulation mechanism of CDF proteins. DATABASE: Structural data are available in RCSB Protein Data Bank under the accession numbers: 6G64, 6G55, 6G5E and 6G6I (for CS, C267S, CS-C267S and W247A, respectively). | ||
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| + | Metal binding to the dynamic cytoplasmic domain of the cation diffusion facilitator (CDF) protein MamM induces a 'locked-in' configuration.,Barber-Zucker S, Hall J, Mangapuram SV, Kass I, Kolusheva S, MacMillan F, Zarivach R, Henn A FEBS J. 2019 Feb 27. doi: 10.1111/febs.14795. PMID:30811856<ref>PMID:30811856</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6g64" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Dsm 6361]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Barber-Zucker, S]] | [[Category: Barber-Zucker, S]] | ||
[[Category: Zarivach, R]] | [[Category: Zarivach, R]] | ||
Current revision
MamM CTD H264A-E289A
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