6gdx | pdb_00006gdx

Structure of CutA from Synechococcus elongatus PCC7942 complexed with 3 molecules of Bis-Tris

spinqualitylabelsall models 6gdx, resolution 1.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6gdx is a 3 chain structure with sequence from Anacystis nidulans r2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BTB Gene: Synpcc7942_2261 (Anacystis nidulans R2) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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.

Proteopedia Page Contributors and Editors (what is this?)

OCA