9sd0 | pdb_00009sd0

The Q102K clinical variant of human bisphosphoglycerate mutase (hBPGM).

spinqualitylabelsall models 9sd0, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9sd0 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: EDO, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease PMGE_HUMAN Defects in BPGM are the cause of bisphosphoglycerate mutase deficiency (BPGMD) [MIM:222800. A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis. Function PMGE_HUMAN Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities. Publication Abstract from PubMed Erythrocyte bisphosphoglycerate mutase (BPGM) plays a major role in regulating hemoglobin (Hb) oxygen affinity by controlling levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Besides its well-documented function in glycolysis, BPGM has been proposed as a regulator of serine pathway flux via 3-phosphoglycerate and as an antimalarial target. In humans, BPGM malfunction reduces intracellular concentrations of 2,3-BPG, producing a leftward shift in the hemoglobin‑oxygen dissociation curve. This shift enhances the affinity of hemoglobin for oxygen, thereby impairing oxygen release to peripheral tissues. The resulting tissue hypoxia induces a compensatory erythropoietic response that clinically manifests as polycythemia/ erythrocytosis, characteristic of familial erythrocytosis type 8 (ECYT8). BPGM deficiency is rare, and a comprehensive study has been conducted in only a few patients with this disease, revealing different missense mutations. In the present study, we structurally characterized clinical variants of human BPGM (hBPGM), i.e., Arg62Gln, Arg90Cys, Arg90His, and Gln102Lys, in order to explore the molecular basis of this rare disease. Analysis of the four structural models and of a new citrate-bound hBPGM structure yielded a partial description of further open/closed conformational changes associated with enzyme activity. New human bisphosphoglycerate mutase structures provide insights into the structural basis of BPGM deficiency and citrate inhibition.,Martinez-Rodriguez S, Torres JM, Sanchez P, Ortega E, Gavira JA Int J Biol Macromol. 2026 Jan;338(Pt 1):149491. doi: , 10.1016/j.ijbiomac.2025.149491. Epub 2025 Dec 5. PMID:41354380 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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