4ARH

X ray structure of the periplasmic zinc binding protein ZinT from Salmonella enterica

Summary for 4ARH

• Entry DOI: 10.2210/pdb4arh/pdb
• Descriptor: METAL-BINDING PROTEIN YODA, SULFATE ION (3 entities in total)
• Functional Keywords: metal binding protein, periplasmic protein
• Biological source: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR
• Total number of polymer chains: 1
• Total formula weight: 22071.57

Authors

Alaleona, F.,Ilari, A.,Battistoni, A.,Petrarca, P.,Chiancone, E. (deposition date: 2012-04-24, release date: 2013-05-08, Last modification date: 2024-11-13)

Primary citation

Ilari, A.,Alaleona, F.,Tria, G.,Petrarca, P.,Battistoni, A.,Zamparelli, C.,Verzili, D.,Falconi, M.,Chiancone, E.
The Salmonella Enterica Zint Structure, Zinc Affinity and Interaction with the High-Affinity Uptake Protein Znua Provide Insight Into the Management of Periplasmic Zinc.
Biochim.Biophys.Acta, 1840:535-, 2014

PubMed Abstract: In Gram-negative bacteria the ZnuABC transporter ensures adequate zinc import in Zn(II)-poor environments, like those encountered by pathogens within the infected host. Recently, the metal-binding protein ZinT was suggested to operate as an accessory component of ZnuABC in periplasmic zinc recruitment. Since ZinT is known to form a ZinT-ZnuA complex in the presence of Zn(II) it was proposed to transfer Zn(II) to ZnuA. The present work was undertaken to test this claim.

PubMed: 24128931
DOI: 10.1016/J.BBAGEN.2013.10.010

Experimental method

X-RAY DIFFRACTION (2.3 Å)