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7BGO

The crystal structure of gene product PA4063 from Pseudomonas aeruginosa in complex with Zn (space group P65)

This is a non-PDB format compatible entry.
Summary for 7BGO
Entry DOI10.2210/pdb7bgo/pdb
Related7AHW 7ALY 7AMX
DescriptorDUF2796 domain-containing protein, ZINC ION (3 entities in total)
Functional Keywordsferredoxin-like, zinc-binding, periplasmic, metal binding protein
Biological sourcePseudomonas aeruginosa
Total number of polymer chains3
Total formula weight58747.74
Authors
Fiorillo, A.,Ilari, A. (deposition date: 2021-01-08, release date: 2021-11-17, Last modification date: 2024-10-16)
Primary citationFiorillo, A.,Battistoni, A.,Ammendola, S.,Secli, V.,Rinaldo, S.,Cutruzzola, F.,Demitri, N.,Ilari, A.
Structure and metal-binding properties of PA4063, a novel player in periplasmic zinc trafficking by Pseudomonas aeruginosa.
Acta Crystallogr D Struct Biol, 77:1401-1410, 2021
Cited by
PubMed Abstract: The capability to obtain essential nutrients in hostile environments is a critical skill for pathogens. Under zinc-deficient conditions, Pseudomonas aeruginosa expresses a pool of metal homeostasis control systems that is complex compared with other Gram-negative bacteria and has only been partially characterized. Here, the structure and zinc-binding properties of the protein PA4063, the first component of the PA4063-PA4066 operon, are described. PA4063 has no homologs in other organisms and is characterized by the presence of two histidine-rich sequences. ITC titration detected two zinc-binding sites with micromolar affinity. Crystallographic characterization, performed both with and without zinc, revealed an α/β-sandwich structure that can be classified as a noncanonical ferredoxin-like fold since it differs in size and topology. The histidine-rich stretches located at the N-terminus and between β3 and β4 are disordered in the apo structure, but a few residues become structured in the presence of zinc, contributing to coordination in one of the two sites. The ability to bind two zinc ions at relatively low affinity, the absence of catalytic cavities and the presence of two histidine-rich loops are properties and structural features which suggest that PA4063 might play a role as a periplasmic zinc chaperone or as a concentration sensor useful for optimizing the response of the pathogen to zinc deficiency.
PubMed: 34726168
DOI: 10.1107/S2059798321009608
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.301 Å)
Structure validation

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数据于2024-11-06公开中

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