2x13
From Proteopedia
The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with ADP and 3phosphoglycerate
Structural highlights
DiseasePGK1_HUMAN Defects in PGK1 are the cause of phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:300653. It is a condition with a highly variable clinical phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy and neurologic involvement. Patients can express one or more of these manifestations.[1] [2] [3] [4] [5] [6] [7] [8] [9] FunctionPGK1_HUMAN In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). Publication Abstract from PubMedEnzymes facilitating the transfer of phosphate groups constitute the most extensive protein families across all kingdoms of life. They make up approximately 10% of the proteins found in the human genome. Understanding the mechanisms by which enzymes catalyze these reactions is essential in characterizing the processes they regulate. Metal fluorides can be used as multifunctional tools to study these enzymes. These ionic species bear the same charge as phosphate and the transferring phosphoryl group and, in addition, allow the enzyme to be trapped in catalytically important states with spectroscopically sensitive atoms interacting directly with active site residues. The ionic nature of these phosphate surrogates also allows their removal and replacement with other analogs. Here, we describe the best practices to obtain these complexes, their use in NMR, X-ray crystallography, cryo-EM, and SAXS and describe a new metal fluoride, scandium tetrafluoride, which has significant anomalous signal using soft X-rays. Metal fluorides-multi-functional tools for the study of phosphoryl transfer enzymes, a practical guide.,Pellegrini E, Juyoux P, von Velsen J, Baxter NJ, Dannatt HRW, Jin Y, Cliff MJ, Waltho JP, Bowler MW Structure. 2024 Jul 22:S0969-2126(24)00270-3. doi: 10.1016/j.str.2024.07.007. PMID:39106858[10] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Homo sapiens | Large Structures | Baxter NJ | Blackburn GM | Bowler MW | Cliff MJ | Hownslow AMH | Marston JPM | Szabo J | Varga AV | Vas M | Waltho JP
