8f8k

The structure of Rv2173 from M. tuberculosis with IPP bound

spinqualitylabelsall models 8f8k, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8f8k is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: ACT, CA, CL, GOL, IPE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GFPPS_MYCTU Catalyzes the sequential condensations of isopentenyl pyrophosphate (IPP) with dimethylallyl diphosphate (DMAPP) to yield geranyl diphosphate (GPP) and with GPP to yield (2E,6E)-farnesyl diphosphate (E,E-FPP). Publication Abstract from PubMed We report structures of the Mycobacterium tuberculosis isoprenyl diphosphate synthase Rv2173 in three forms: apo and two substrate-bound forms [isoprenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP)]. The protein possesses a canonical all-alpha-helical trans-isoprenyl diphosphate synthase fold that is dimeric in each form. There are some differences between the structures: the IPP-bound form shows IPP bound in the DMAPP/allylic substrate-binding site with three divalent metal ions bound around the IPP and the complete C-terminus closing around the active site, while the apo and DMAPP-bound forms are more open, with some of the C-terminal region disordered, supporting suggestions that the C-terminus is important in substrate entry/product exit. In the DMAPP form DMAPP occupies the expected allylic substrate site, but only two metal ions are associated with the binding, with the DMAPP diphosphates adopting a slightly different binding pose compared with IPP in the same site, and the third metal-binding site is unoccupied. In no case is the IPP binding site occupied by IPP. There has been some uncertainty regarding product length for Rv2173, with variable lengths being reported. In the structures reported here, the ;capping' residue at the bottom of the binding cavity is tryptophan and comparison with other IPP synthases suggests that the structure of Rv2173 is most consistent with a C(10)-C(15) final product size. Structures of Mycobacterium tuberculosis isoprenyl diphosphate synthase Rv2173 in substrate-bound forms.,Titterington JA, Ho NAT, Beasley CPH, Mann F, Baker EN, Allison TM, Johnston JM Acta Crystallogr F Struct Biol Commun. 2025 May 1;81(Pt 5):193-200. doi: , 10.1107/S2053230X25002298. Epub 2025 Apr 1. PMID:40166974 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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