6CK1

Crystal structure of Paracoccus denitrificans AztD

Summary for 6CK1

• Entry DOI: 10.2210/pdb6ck1/pdb
• Descriptor: A1B2F4 protein, ZINC ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: zinc, beta propeller, periplasm, metal binding protein
• Biological source: Paracoccus denitrificans (strain Pd 1222)
• Total number of polymer chains: 4
• Total formula weight: 173521.16

Authors

Yukl, E.T. (deposition date: 2018-02-27, release date: 2019-03-06, Last modification date: 2024-10-30)

Primary citation

Neupane, D.P.,Fullam, S.H.,Chacon, K.N.,Yukl, E.T.
Crystal structures of AztD provide mechanistic insights into direct zinc transfer between proteins.
Commun Biol, 2:308-308, 2019

PubMed Abstract: Zinc acquisition from limited environments is critical for bacterial survival and pathogenesis. AztD has been identified as a periplasmic or cell surface zinc-binding protein in numerous bacterial species. In , AztD can transfer zinc directly to AztC, the solute binding protein for a zinc-specific ATP-binding cassette transporter system, suggesting a role in zinc acquisition and homeostasis. Here, we present the first cry stal structures of AztD from and tbe human pathogen , revealing a beta-propeller fold and two high-affinity zinc-binding sites that are highly conserved among AztD homologs. These structures combined with transfer assays using WT and mutant proteins provide rare insight into the mechanism of direct zinc transfer from one protein to another. Given the importance of zinc import to bacterial pathogenesis, these insights may prove valuable to the development of zinc transfer inhibitors as antibiotics.

PubMed: 31428696
DOI: 10.1038/s42003-019-0542-z

Experimental method

X-RAY DIFFRACTION (2.15 Å)