5nlc

Structure of PipY, the COG0325 family member of Synechococcus elongatus PCC7942,without PLP

spinqualitylabelsall models 5nlc, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nlc is a 2 chain structure with sequence from Synechococcus elongatus PCC 7942 = FACHB-805. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q31LH9_SYNE7 Publication Abstract from PubMed 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. Studies on cyanobacterial protein PipY shed light on structure, potential functions, and vitamin B6 -dependent epilepsy.,Tremino L, Forcada-Nadal A, Contreras A, Rubio V FEBS Lett. 2017 Sep 15. doi: 10.1002/1873-3468.12841. PMID:28914444 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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