6M7W

Role of the highly conserved G68 residue in the yeast phosphorelay protein Ypd1: implications for interactions between histidine phosphotransfer (HPt) and response regulator proteins

Summary for 6M7W

• Entry DOI: 10.2210/pdb6m7w/pdb
• Descriptor: Phosphorelay intermediate protein YPD1 (2 entities in total)
• Functional Keywords: g68q mutant, hpt, yeast phosphorelay, transferase
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 19258.73

Authors

Menon, S.K.,Soni, K.S.,West, A.H. (deposition date: 2018-08-21, release date: 2019-02-06, Last modification date: 2023-10-11)

Primary citation

Kennedy, E.N.,Hebdon, S.D.,Menon, S.K.,Foster, C.A.,Copeland, D.M.,Xu, Q.,Janiak-Spens, F.,West, A.H.
Role of the highly conserved G68 residue in the yeast phosphorelay protein Ypd1: implications for interactions between histidine phosphotransfer (HPt) and response regulator proteins.
BMC Biochem., 20:1-1, 2019

PubMed Abstract: Many bacteria and certain eukaryotes utilize multi-step His-to-Asp phosphorelays for adaptive responses to their extracellular environments. Histidine phosphotransfer (HPt) proteins function as key components of these pathways. HPt proteins are genetically diverse, but share a common tertiary fold with conserved residues near the active site. A surface-exposed glycine at the H + 4 position relative to the phosphorylatable histidine is found in a significant number of annotated HPt protein sequences. Previous reports demonstrated that substitutions at this position result in diminished phosphotransfer activity between HPt proteins and their cognate signaling partners.

PubMed: 30665347
DOI: 10.1186/s12858-019-0104-5

Experimental method

X-RAY DIFFRACTION (1.98 Å)