6XPN

Z-loop Deletion Mutant of AztC from Paracoccus denitrificans

Summary for 6XPN

• Entry DOI: 10.2210/pdb6xpn/pdb
• Descriptor: Periplasmic solute binding protein, ZINC ION (3 entities in total)
• Functional Keywords: zinc, solute binding protein, abc transporter, metal binding protein
• Biological source: Paracoccus denitrificans (strain Pd 1222)
• Total number of polymer chains: 2
• Total formula weight: 63329.85

Authors

Yukl, E.T. (deposition date: 2020-07-08, release date: 2020-08-26, Last modification date: 2024-10-09)

Primary citation

Meni, A.,Yukl, E.T.
Structural Features Mediating Zinc Binding and Transfer in the AztABCD Zinc Transporter System.
Biomolecules, 10:-, 2020

PubMed Abstract: Many bacteria require ATP binding cassette (ABC) transporters for the import of the essential metal zinc from limited environments. These systems rely on a periplasmic or cell-surface solute binding protein (SBP) to bind zinc with high affinity and specificity. AztABCD is one such zinc transport system recently identified in a large group of diverse bacterial species. In addition to a classical SBP (AztC), the operon also includes a periplasmic metallochaperone (AztD) shown to transfer zinc directly to AztC. Crystal structures of both proteins from have been solved and suggest several structural features on each that may be important for zinc binding and transfer. Here we determine zinc binding affinity, dissociation kinetics, and transfer kinetics for several deletion mutants as well as a crystal structure for one of them. The results indicate specific roles for loop structures on AztC and an N-terminal motif on AztD in zinc binding and transfer. These data are consistent with a structural transfer model proposed previously and provide further mechanistic insight into the processes of zinc binding and transfer.

PubMed: 32781785
DOI: 10.3390/biom10081156

Experimental method

X-RAY DIFFRACTION (2.26 Å)