|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Structure of Holo AztC== | | ==Structure of Holo AztC== |
| - | <StructureSection load='5w57' size='340' side='right' caption='[[5w57]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='5w57' size='340' side='right'caption='[[5w57]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5w57]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pardp Pardp]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4xrv 4xrv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W57 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W57 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5w57]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans_PD1222 Paracoccus denitrificans PD1222]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4xrv 4xrv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W57 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5w56|5w56]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pden_1597 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318586 PARDP])</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=5w57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w57 OCA], [https://pdbe.org/5w57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w57 RCSB], [https://www.ebi.ac.uk/pdbsum/5w57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w57 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=5w57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w57 OCA], [http://pdbe.org/5w57 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w57 RCSB], [http://www.ebi.ac.uk/pdbsum/5w57 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w57 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A1B2F3_PARDP A1B2F3_PARDP] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pardp]] | + | [[Category: Large Structures]] |
| - | [[Category: Avalos, D]] | + | [[Category: Paracoccus denitrificans PD1222]] |
| - | [[Category: Yukl, E T]] | + | [[Category: Avalos D]] |
| - | [[Category: Abc transporter]] | + | [[Category: Yukl ET]] |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Solute binding protein]]
| + | |
| - | [[Category: Zinc]]
| + | |
| Structural highlights
Function
A1B2F3_PARDP
Publication Abstract from PubMed
Bacteria can acquire the essential metal zinc from extremely zinc-limited environments by using ATP-binding cassette (ABC) transporters. These transporters are critical virulence factors relying on specific and high-affinity binding of zinc by a periplasmic solute-binding protein (SBP). As such, the mechanisms of zinc binding and release among bacterial SBPs are of considerable interest as antibacterial drug targets. Zinc SBPs are characterized by a flexible loop near the high-affinity zinc-binding site. The function of this structure is not always clear, and its flexibility has thus far prevented structural characterization by X-ray crystallography. Here, we present intact structures for the zinc-specific SBP AztC from the bacterium Paracoccus denitrificans in the zinc-bound and the apo states. A comparison of these structures revealed that zinc loss prompts significant structural rearrangements mediated by the formation of a sodium-binding site in the apo structure. We further show that the AztC flexible loop has no impact on zinc-binding affinity, stoichiometry, or protein structure, yet is essential for zinc transfer from the metallochaperone AztD. We also found that three His residues in the loop appear to temporarily coordinate zinc and then convey it to the high-affinity binding site. Consistent with this, mutation of any of these residues to Ala abrogated zinc transfer from AztD. Our structural and mechanistic findings conclusively identify a role for the AztC flexible loop in zinc acquisition from the metallochaperone AztD and yield critical insights into metal binding by AztC from both solution and AztD. These proteins are highly conserved in human pathogens, making this work potentially useful to the development of novel antibiotics.
Mechanisms of zinc binding to the solute binding protein AztC and transfer from the metallochaperone AztD.,Neupane DP, Avalos D, Fullam S, Roychowdhury H, Yukl ET J Biol Chem. 2017 Sep 7. pii: jbc.M117.804799. doi: 10.1074/jbc.M117.804799. PMID:28887302[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Neupane DP, Avalos D, Fullam S, Roychowdhury H, Yukl ET. Mechanisms of zinc binding to the solute binding protein AztC and transfer from the metallochaperone AztD. J Biol Chem. 2017 Sep 7. pii: jbc.M117.804799. doi: 10.1074/jbc.M117.804799. PMID:28887302 doi:http://dx.doi.org/10.1074/jbc.M117.804799
|
