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| | <StructureSection load='4ayh' size='340' side='right'caption='[[4ayh]], [[Resolution|resolution]] 2.52Å' scene=''> | | <StructureSection load='4ayh' size='340' side='right'caption='[[4ayh]], [[Resolution|resolution]] 2.52Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ayh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AYH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ayh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AYH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.52Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4arh|4arh]], [[4aw8|4aw8]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4ayh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ayh OCA], [https://pdbe.org/4ayh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ayh RCSB], [https://www.ebi.ac.uk/pdbsum/4ayh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ayh ProSAT]</span></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=4ayh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ayh OCA], [https://pdbe.org/4ayh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ayh RCSB], [https://www.ebi.ac.uk/pdbsum/4ayh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ayh ProSAT]</span></td></tr> |
| | </table> | | </table> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus cholerae-suis smith 1894]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alaleona, F]] | + | [[Category: Salmonella enterica]] |
| - | [[Category: Battistoni, A]] | + | [[Category: Alaleona F]] |
| - | [[Category: Chiancone, E]] | + | [[Category: Battistoni A]] |
| - | [[Category: Ilari, A]] | + | [[Category: Chiancone E]] |
| - | [[Category: Petrarca, P]] | + | [[Category: Ilari A]] |
| - | [[Category: Metal binding protein]]
| + | [[Category: Petrarca P]] |
| - | [[Category: Metal-binding protein]]
| + | |
| - | [[Category: Zinc transport]]
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| Structural highlights
Publication Abstract from PubMed
BACKGROUND: In Gram-negative bacteria the ZnuABC transporter ensures adequate zinc import in Zn(II)-poor environments, like those encountered by pathogens within the infected host. Recently, the metal-binding protein ZinT was suggested to operate as an accessory component of ZnuABC in periplasmic zinc recruitment. Since ZinT is known to form a ZinT-ZnuA complex in the presence of Zn(II) it was proposed to transfer Zn(II) to ZnuA. The present work was undertaken to test this claim. METHODS: ZinT and its structural relationship with ZnuA have been characterized by multiple biophysical techniques (X-ray crystallography, SAXS, analytical ultracentrifugation, fluorescence spectroscopy). RESULTS: The metal-free and metal-bound crystal structures of Salmonella enterica ZinT show one Zn(II) binding site and limited structural changes upon metal removal. Spectroscopic titrations with Zn(II) yield a KD value of 22+/-2nM for ZinT, while those with ZnuA point to one high affinity (KD<20nM) and one low affinity Zn(II) binding site (KD in the micromolar range). Sedimentation velocity experiments established that Zn(II)-bound ZinT interacts with ZnuA, whereas apo-ZinT does not. The model of the ZinT-ZnuA complex derived from small angle X-ray scattering experiments points to a disposition that favors metal transfer as the metal binding cavities of the two proteins face each other. CONCLUSIONS: ZinT acts as a Zn(II)-buffering protein that delivers Zn(II) to ZnuA. GENERAL SIGNIFICANCE: Knowledge of the ZinT-ZnuA relationship is crucial for understanding bacterial Zn(II) uptake.
The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc.,Ilari A, Alaleona F, Tria G, Petrarca P, Battistoni A, Zamparelli C, Verzili D, Falconi M, Chiancone E Biochim Biophys Acta. 2014 Jan;1840(1):535-44. doi: 10.1016/j.bbagen.2013.10.010., Epub 2013 Oct 12. PMID:24128931[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ilari A, Alaleona F, Tria G, Petrarca P, Battistoni A, Zamparelli C, Verzili D, Falconi M, Chiancone E. The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc. Biochim Biophys Acta. 2014 Jan;1840(1):535-44. doi: 10.1016/j.bbagen.2013.10.010., Epub 2013 Oct 12. PMID:24128931 doi:http://dx.doi.org/10.1016/j.bbagen.2013.10.010
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