4G9P

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

Summary for 4G9P

• Entry DOI: 10.2210/pdb4g9p/pdb
• Descriptor: 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase, IRON/SULFUR CLUSTER, 2C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE, ... (7 entities in total)
• Functional Keywords: oxidoreductase, isoprenoid biosynthesis, non mevalonate pathway, iron-sulphur-cluster, tim-barrel, mecpp
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 45411.30

Authors

Rekittke, I.,Jomaa, H.,Ermler, U. (deposition date: 2012-07-24, release date: 2012-09-26, Last modification date: 2024-02-28)

Primary citation

Rekittke, I.,Jomaa, H.,Ermler, U.
Structure of the GcpE (IspG)-MEcPP complex from Thermus thermophilus.
Febs Lett., 586:3452-3457, 2012

PubMed Abstract: 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 1.55Å resolution provides valuable information about the catalytic mechanism and for rational inhibitor design. MEcPP binding inside the TIM-barrel funnel induces a 60° 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.

PubMed: 22967895
DOI: 10.1016/j.febslet.2012.07.070

Experimental method

X-RAY DIFFRACTION (1.55 Å)