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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography	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 Khaled A. Selim , Lorena Tremino , Clara Marco-marin , Vikram Alva , Javier Espinosa , Asunción Contreras , Marcus D. Hartmann , Karl Forchhammer , Vicente Rubio The Febs Journal 276 DOI: 10.1111/febs.15464 Diamond Proposal Number(s): [20229] Open Access Show Abstract ▼ Abstract: The PII‐like protein CutA is annotated as being involved in Cu2+ 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 Cu2+. 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 their 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 Cu2+ 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.	Jul 2020
I03-Macromolecular Crystallography	Studies on cyanobacterial protein PipY shed light on structure, potential functions, and vitamin B 6 -dependent epilepsy Lorena Tremiño , Alicia Forcada-nadal , Asunción Contreras , Vicente Rubio Febs Letters 109 DOI: 10.1002/1873-3468.12841 Diamond Proposal Number(s): [14739] Show Abstract ▼ Abstract: The Synechococcus elongatus COG0325 gene pipY functionally interacts with the nitrogen regulatory gene pipX. As a first step toward a molecular understanding of such interactions, we characterized PipY. This 221-residue protein is monomeric and hosts pyridoxal phosphate (PLP), binding it with limited affinity and losing it upon incubation with D-cycloserine. PipY crystal structures with and without PLP reveal a single-domain monomer folded as the TIM barrel of type-III fold PLP enzymes, with PLP highly exposed, fitting a role for PipY in PLP homeostasis. The mobile PLP phosphate-anchoring C-terminal helix might act as a trigger for PLP exchange. Exploiting the universality of COG0325 functions, we used PipY in site-directed mutagenesis studies to shed light on disease causation by epilepsy-associated mutations in the human COG0325 gene PROSC.	Sep 2017

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