5NLC
Structure of PipY, the COG0325 family member of Synechococcus elongatus PCC7942,without PLP
Summary for 5NLC
| Entry DOI | 10.2210/pdb5nlc/pdb |
| Descriptor | PipY, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | modified tim barrel, fold type iii plp-protein, vitamin b6, pyridoxal phosphate, plp-binding protein |
| Biological source | Synechococcus elongatus (strain PCC 7942) |
| Total number of polymer chains | 2 |
| Total formula weight | 50694.79 |
| Authors | Tremino, L.,Forcada-Nadal, A.,Contreras, A.,Rubio, V. (deposition date: 2017-04-04, release date: 2017-09-13, Last modification date: 2024-01-17) |
| Primary citation | Tremino, L.,Forcada-Nadal, A.,Contreras, A.,Rubio, V. Studies on cyanobacterial protein PipY shed light on structure, potential functions, and vitamin B6 -dependent epilepsy. FEBS Lett., 591:3431-3442, 2017 Cited by PubMed 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. PubMed: 28914444DOI: 10.1002/1873-3468.12841 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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