6ixi

structure of Cd-bound periplasmic metal binding protein from candidatus liberibacter asiaticus

spinqualitylabelsall models 6ixi, resolution 2.07Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ixi is a 1 chain structure with sequence from Candidatus Liberibacter asiaticus str. psy62. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.07Å Ligands: ACT, CD, GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C6XF58_LIBAP Publication Abstract from PubMed Candidatus Liberibacter asiaticus (CLas), a phloem-limited unculturable Gram-negative bacterium, causes citrus greening disease. The proteome analysis of CLas showed the presence of a heavy metal permease and Co/Zn/Cd cation exporter system. However, there is no designated metal uptake protein specific for the heavy metal permease in CLas. One of the metal uptake proteins, designated as CLas-ZnuA2, in our previous studies, showed a lower metal-binding affinity for Mn2+ and Zn2+ and was postulated to bind and transport metals rather non-specifically. The present study focused on the characterization of the heavy metal binding properties of CLas-ZnuA2 using SPR, CD, DSC and crystallographic studies. The crystal structure analysis of Cd2+ bound CLas-ZnuA2 showed octahedral geometry for Cd2+ binding as compared to a non-preferred square-pyramidal geometry for Mn2+ and Zn2+ binding in earlier reported crystal structures. In SPR analysis, the binding affinities of 4.7 x 10-6 M, 7.2 x 10-6 M, 5.3 x 10-5 M and 4.3 x 10-5 M for Hg2+, Cd2+, Ba2+ and Co2+ respectively were higher as compared to earlier reported values for Mn2+ and Zn2+. Likewise, CD and DSC analysis showed relatively higher thermal stability for CLas-ZnuA2 on heavy metal binding. Taken together with the expression of the permease and exporter system for heavy metals, our results indicate that CLas-ZnuA2 may be involved in sequestering and transport of various transition divalent metals in environmentally stressed conditions. Characterization of the heavy metal binding properties of periplasmic metal uptake protein CLas-ZnuA2.,Kumar P, Dalal V, Sharma N, Kokane S, Ghosh DK, Kumar P, Sharma AK Metallomics. 2020 Feb 26;12(2):280-289. doi: 10.1039/c9mt00200f. PMID:31853532 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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