5lu7

Heptose isomerase GmhA mutant - D61A

spinqualitylabelsall models 5lu7, resolution 1.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5lu7 is a 4 chain structure with sequence from Burkholderia pseudomallei K96243. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.92Å Ligands: EDO, M7P, PG4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GMHA_BURPS Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. Publication Abstract from PubMed Cooperativity is a feature many multimeric proteins use to control activity. Here we show that the bacterial heptose isomerase GmhA displays homotropic positive and negative cooperativity among its four protomers. Most similar proteins achieve this through conformational changes: GmhA instead employs a delicate network of hydrogen bonds, and couples pairs of active sites controlled by a unique water channel. This network apparently raises the Lewis acidity of the catalytic zinc, thus increasing the activity at one active site at the cost of preventing substrate from adopting a reactive conformation at the paired negatively cooperative site - a "half-site" behavior. Our study establishes the principle that multimeric enzymes can exploit this cooperativity without conformational changes to maximize their catalytic power and control. More broadly, this subtlety by which enzymes regulate functions could be used to explore new inhibitor design strategies. A half-site multimeric enzyme achieves its cooperativity without conformational changes.,Vivoli M, Pang J, Harmer NJ Sci Rep. 2017 Nov 28;7(1):16529. doi: 10.1038/s41598-017-16421-2. PMID:29184087 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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