3byr: Difference between revisions
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==Mode of Action of a Putative Zinc Transporter CzrB (Zn form)== | ==Mode of Action of a Putative Zinc Transporter CzrB (Zn form)== | ||
<StructureSection load='3byr' size='340' side='right' caption='[[3byr]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='3byr' size='340' side='right' caption='[[3byr]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3byp|3byp]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3byp|3byp]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">czrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">czrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])</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=3byr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3byr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3byr RCSB], [http://www.ebi.ac.uk/pdbsum/3byr PDBsum]</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=3byr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3byr OCA], [http://pdbe.org/3byr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3byr RCSB], [http://www.ebi.ac.uk/pdbsum/3byr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3byr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3byr ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3byr" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 13:13, 11 August 2016
Mode of Action of a Putative Zinc Transporter CzrB (Zn form)Mode of Action of a Putative Zinc Transporter CzrB (Zn form)
Structural highlights
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 PubMedThe crystal structures of the cytoplasmic domain of the putative zinc transporter CzrB in the apo and zinc-bound forms reported herein are consistent with the protein functioning in vivo as a homodimer. NMR, X-ray scattering, and size-exclusion chromatography provide support for dimer formation. Full-length variants of CzrB in the apo and zinc-loaded states were generated by homology modeling with the Zn2+/H+ antiporter YiiP. The model suggests a way in which zinc binding to the cytoplasmic fragment creates a docking site to which a metallochaperone can bind for delivery and transport of its zinc cargo. Because the cytoplasmic domain may exist in the cell as an independent, soluble protein, a proposal is advanced that it functions as a metallochaperone and that it regulates the zinc-transporting activity of the full-length protein. The latter requires that zinc binding becomes uncoupled from the creation of a metallochaperone-docking site on CzrB. Insights into the mode of action of a putative zinc transporter CzrB in Thermus thermophilus.,Cherezov V, Hofer N, Szebenyi DM, Kolaj O, Wall JG, Gillilan R, Srinivasan V, Jaroniec CP, Caffrey M Structure. 2008 Sep 10;16(9):1378-88. PMID:18786400[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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