6t7e

PII-like protein CutA from Nostoc sp. PCC7120 in complex with MESPII-like protein CutA from Nostoc sp. PCC7120 in complex with MES

Structural highlights 6t7e is a 6 chain structure with sequence from Nostoc sp. PCC 7120 = FACHB-418. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.45Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8YL42_NOSS1 Publication Abstract from PubMed The PII-like protein CutA is annotated as being involved in Cu(2+) tolerance, based on analysis of Escherichia coli mutants. However, the precise cellular function of CutA remains unclear. Our bioinformatic analysis reveals that CutA proteins are universally distributed across all domains of life. Based on sequence-based clustering, we chose representative cyanobacterial CutA proteins for physiological, biochemical and structural characterization and examined their involvement in heavy metal tolerance, by generating CutA mutants in filamentous Nostoc sp. and in unicellular Synechococcus elongatus. However, we were unable to find any involvement of cyanobacterial CutA in metal tolerance under various conditions. This prompted us to re-examine experimentally the role of CutA in protecting E. coli from Cu(2+) . Since we found no effect on copper-tolerance, we conclude that CutA plays a different role that is not involved in metal protection. We resolved high-resolution CutA structures from Nostoc and S elongatus. Similarly to its counterpart from E.coli and to canonical PII proteins, cyanobacterial CutA proteins are trimeric in solution and in crystal structure; however, no binding affinity for small signaling molecules or for Cu(2+) could be detected. The clefts between the CutA subunits, corresponding to the binding pockets of PII proteins, are formed by conserved aromatic and charged residues, suggesting a conserved binding/signaling function for CutA. In fact, we find binding of organic Bis-Tris/MES molecules in CutA crystal structures, revealing a strong tendency of these pockets to accommodate cargo. This highlights the need to search for the potential physiological ligands and for their signaling functions upon binding to CutA. Functional and structural characterization of PII-like protein CutA does not support involvement in heavy metal tolerance and hints at a small-molecule carrying/signaling role.,Selim KA, Tremino L, Marco-Marin C, Alva V, Espinosa J, Contreras A, Hartmann MD, Forchhammer K, Rubio V FEBS J. 2020 Jun 29. doi: 10.1111/febs.15464. PMID:32599651 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CutA1 3D structures

spinqualitylabelsall models 6t7e, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image