Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2017 Sep 15. doi: 10.1002/1873-3468.12841. PMID:28914444 doi:http://dx.doi.org/10.1002/1873-3468.12841