Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc.
Journal, issue, pages	Biochim Biophys Acta, Vol. 1840, Issue 1, Page 535-544, Year 2014
Publish date	Oct 12, 2013
Authors	Andrea Ilari / Flaminia Alaleona / Giancarlo Tria / Patrizia Petrarca / Andrea Battistoni / Carlotta Zamparelli / Daniela Verzili / Mattia Falconi / Emilia Chiancone /
PubMed Abstract	BACKGROUND: 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 ...BACKGROUND: 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. METHODS: ZinT and its structural relationship with ZnuA have been characterized by multiple biophysical techniques (X-ray crystallography, SAXS, analytical ultracentrifugation, fluorescence spectroscopy). RESULTS: The metal-free and metal-bound crystal structures of Salmonella enterica ZinT show one Zn(II) binding site and limited structural changes upon metal removal. Spectroscopic titrations with Zn(II) yield a KD value of 22±2nM for ZinT, while those with ZnuA point to one high affinity (KD<20nM) and one low affinity Zn(II) binding site (KD in the micromolar range). Sedimentation velocity experiments established that Zn(II)-bound ZinT interacts with ZnuA, whereas apo-ZinT does not. The model of the ZinT-ZnuA complex derived from small angle X-ray scattering experiments points to a disposition that favors metal transfer as the metal binding cavities of the two proteins face each other. CONCLUSIONS: ZinT acts as a Zn(II)-buffering protein that delivers Zn(II) to ZnuA. GENERAL SIGNIFICANCE: Knowledge of the ZinT-ZnuA relationship is crucial for understanding bacterial Zn(II) uptake.
External links	Biochim Biophys Acta / PubMed:24128931
Methods	SAS (X-ray synchrotron) / X-ray diffraction
Resolution	2 - 2.52 Å
Structure data	SASDA35: SeZinT-SeZnuA complex (High-affinity zinc transporter periplasmic component, ZinT + Zinc/cadmium-binding protein, SeZnuA) Method: SAXS/SANS PDB-4arh: X ray structure of the periplasmic zinc binding protein ZinT from Salmonella enterica Method: X-RAY DIFFRACTION / Resolution: 2.3 Å PDB-4aw8: X-ray structure of ZinT from Salmonella enterica in complex with zinc ion and PEG Method: X-RAY DIFFRACTION / Resolution: 2.0 Å PDB-4ayh: The X-ray structure of zinc bound ZinT Method: X-RAY DIFFRACTION / Resolution: 2.52 Å
Chemicals	ChemComp-SO4: SULFATE ION ChemComp-HOH: WATER ChemComp-ZN: Unknown entry ChemComp-PG6: 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE ChemComp-NA: Unknown entry
Source	Salmonella enterica subsp. enterica serovar nchanga (bacteria) Salmonella enterica subsp. enterica serovar enteritidis (bacteria) salmonella enterica subsp. enterica serovar (bacteria) salmonella enterica (bacteria)
Keywords	METAL BINDING PROTEIN / PERIPLASMIC PROTEIN / ZINC TRANSPORT / METAL-BINDING PROTEIN