5zha

Structure of Y68F mutant Mn-Bound periplasmic metal binding protein from candidatus liberibacter asiaticus

spinqualitylabelsall models 5zha, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5zha 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 1.84Å Ligands: ACT, GOL, MN, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C6XF58_LIBAP Publication Abstract from PubMed The subtle internal communications through an intricate network of interactions play a key role in metal-binding and release in periplasmic metal uptake proteins of cluster A-I family, a component of ABC transport system. These proteins have evolved different mechanisms of metal-binding and release through sequence and thereby structure-function divergence. The CLas-ZnuA2 from Candidatus Liberibacter asiaticus (CLA), in previous studies, showed a lower metal-binding affinity. The subtle communications within and between domains from crystal structure analysis revealed that protein seems to prefer a metal-free state. The unique features of CLas-ZnuA2 included a highly restrained loop L3 and presence of a proline in linker helix. In present work, S38A and Y68F mutants were studied as they play an important role during metal-binding in CLas-ZnuA2. The mutations in linker helix could not be studied as the expressed protein was not soluble and in most cases degraded with time. The crystal structure analysis of (S38A and Y68F) mutants in metal-free and metal-bound forms showed variations in interactions, an increase in number of alternate conformations and distortions in secondary structure elements, despite a similar overall structure, suggesting alterations in internal communications. The results suggested that any change in critical residues could alter the subtle internal communications and result in disturbing the fine-tuned structure required for optimal functioning. The analysis of subtle internal communications through mutation studies in periplasmic metal uptake protein CLas-ZnuA2.,Saini G, Sharma N, Dalal V, Warghane A, Ghosh DK, Kumar P, Sharma AK J Struct Biol. 2018 Nov;204(2):228-239. doi: 10.1016/j.jsb.2018.08.013. Epub 2018, Aug 17. PMID:30125692 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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