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| | <StructureSection load='6pgi' size='340' side='right'caption='[[6pgi]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='6pgi' size='340' side='right'caption='[[6pgi]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6pgi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"alcaligenes_bronchicanis"_(ferry_1911)_haupt_1935 "alcaligenes bronchicanis" (ferry 1911) haupt 1935]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PGI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PGI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6pgi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_bronchiseptica Bordetella bronchiseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PGI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</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]] 3.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BB2405 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=518 "Alcaligenes bronchicanis" (Ferry 1911) Haupt 1935])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></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=6pgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pgi OCA], [http://pdbe.org/6pgi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pgi RCSB], [http://www.ebi.ac.uk/pdbsum/6pgi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pgi 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=6pgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pgi OCA], [https://pdbe.org/6pgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pgi RCSB], [https://www.ebi.ac.uk/pdbsum/6pgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pgi ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0H3LM39_BORBR A0A0H3LM39_BORBR] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Bordetella bronchiseptica]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hu, J]] | + | [[Category: Hu J]] |
| - | [[Category: Logan, T]] | + | [[Category: Logan T]] |
| - | [[Category: Sui, D]] | + | [[Category: Sui D]] |
| - | [[Category: Zhang, C]] | + | [[Category: Zhang C]] |
| - | [[Category: Zhang, T]] | + | [[Category: Zhang T]] |
| - | [[Category: Binuclear metal cluster]]
| + | |
| - | [[Category: Cadmium]]
| + | |
| - | [[Category: Metal transporter]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Zinc]]
| + | |
| - | [[Category: Zip]]
| + | |
| Structural highlights
Function
A0A0H3LM39_BORBR
Publication Abstract from PubMed
Metal clusters are exploited by numerous metalloenzymes for catalysis, but it is not common to utilize a metal cluster for substrate transport across membrane. The recent crystal structure of a prototypic Zrt-/Irt-like protein (ZIP) metal transporter from Bordetella bronchiseptica (BbZIP) revealed an unprecedented binuclear metal center (BMC) within the transport pathway. Here, through a combination of bioinformatics, biochemical and structural approaches, we concluded that the two physically associated metal-binding sites in the BMC of human ZIP4 (hZIP4) zinc transporter exert different functions: one conserved transition metal-binding site acts as the transport site essential for activity, whereas the variable metal-binding site is required for hZIP4's optimal activity presumably by serving as a secondary transport site and modulating the properties of the primary transport site. Sequential soaking experiments on BbZIP crystals clarified the process of metal release from the BMC to the bulky solvent. This work provides important insights into the transport mechanism of the ZIPs broadly involved in transition metal homeostasis and signaling, and also a paradigm on a novel function of metal cluster in metalloproteins.
Asymmetric functions of a binuclear metal center within the transport pathway of a human zinc transporter ZIP4.,Zhang T, Sui D, Zhang C, Cole L, Hu J FASEB J. 2020 Jan;34(1):237-247. doi: 10.1096/fj.201902043R. Epub 2019 Nov 21. PMID:31914589[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang T, Sui D, Zhang C, Cole L, Hu J. Asymmetric functions of a binuclear metal center within the transport pathway of a human zinc transporter ZIP4. FASEB J. 2020 Jan;34(1):237-247. doi: 10.1096/fj.201902043R. Epub 2019 Nov 21. PMID:31914589 doi:http://dx.doi.org/10.1096/fj.201902043R
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