4g9p

Structure of the GcpE-MEcPP (IspG) complex from Thermus thermophilus

spinqualitylabelsall models 4g9p, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4g9p is a 1 chain structure with sequence from Thermus thermophilus HB27. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.55Å Ligands: CDI, CL, K, MES Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ISPG_THET2 Publication Abstract from PubMed Isoprenoid precursor biosynthesis occurs through the mevalonate or the methylerythritol phosphate (MEP) pathway, used i.e., by humans and by many human pathogens, respectively. In the MEP pathway, 2-C-methyl-d-erythritol-2,4-cyclo-diphosphate (MEcPP) is converted to (E)-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate (HMBPP) by the iron-sulfur cluster enzyme HMBPP synthase (GcpE). The presented X-ray structure of the GcpE-MEcPP complex from Thermus thermophilus at 1.55A resolution provides valuable information about the catalytic mechanism and for rational inhibitor design. MEcPP binding inside the TIM-barrel funnel induces a 60 degrees rotation of the [4Fe-4S] cluster containing domain onto the TIM-barrel entrance. The apical iron of the [4Fe-4S] cluster ligates with the C3 oxygen atom of MEcPP. Structure of the GcpE (IspG)-MEcPP complex from Thermus thermophilus.,Rekittke I, Jomaa H, Ermler U FEBS Lett. 2012 Sep 21;586(19):3452-7. doi: 10.1016/j.febslet.2012.07.070. Epub, 2012 Aug 9. PMID:22967895 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also IspG

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