6CMK
Crystal structure of Citrobacter koseri AztD
Summary for 6CMK
| Entry DOI | 10.2210/pdb6cmk/pdb |
| Descriptor | AztD protein, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ZINC ION, ... (7 entities in total) |
| Functional Keywords | zinc, beta propeller, periplasm, metal binding protein |
| Biological source | Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) |
| Total number of polymer chains | 2 |
| Total formula weight | 92091.42 |
| Authors | Yukl, E.T. (deposition date: 2018-03-05, release date: 2019-03-13, Last modification date: 2024-10-23) |
| 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 Cited by 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: 31428696DOI: 10.1038/s42003-019-0542-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.732 Å) |
Structure validation
Download full validation report
