1P0K

IPP:DMAPP isomerase type II apo structure

Summary for 1P0K

• Entry DOI: 10.2210/pdb1p0k/pdb
• Related: 1P0N
• Descriptor: Isopentenyl-diphosphate delta-isomerase, PHOSPHATE ION (3 entities in total)
• Functional Keywords: terpene biosynthesis, isopentenyl diphosphate, dimethylallyl diphosphate, isomerase, flavoprotein
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm (By similarity): P50740
• Total number of polymer chains: 2
• Total formula weight: 74714.93

Authors

Steinbacher, S.,Kaiser, J.,Gerhardt, S.,Eisenreich, W.,Huber, R.,Bacher, A.,Rohdich, F. (deposition date: 2003-04-10, release date: 2003-06-17, Last modification date: 2024-03-13)

Primary citation

Steinbacher, S.,Kaiser, J.,Gerhardt, S.,Eisenreich, W.,Huber, R.,Bacher, A.,Rohdich, F.
Crystal Structure of the Type II Isopentenyl Diphosphate:Dimethylallyl Diphosphate Isomerase from Bacillus subtilis
J.Mol.Biol., 329:973-982, 2003

PubMed Abstract: Two types of isopentenyl diphosphate:dimethylallyl diphosphate isomerases (IDI) have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. Here, we report the first structure of an IDI-2 from Bacillus subtilis at 1.9A resolution in the ligand-free form and of the FMN-bound form at 2.8A resolution. The enzyme is an octamer that forms a D4 symmetrical open, cage-like structure. The monomers of 45 kDa display a classical TIM barrel fold. FMN is bound only with very moderate affinity and is therefore completely lost during purification. However, the enzyme can be reconstituted in the crystals by soaking with FMN. Three glycine-rich sequence stretches that are characteristic for IDI-2 participate in FMN binding within the interior of the cage. Regions harboring strictly conserved residues that are implicated in substrate binding or catalysis remain largely disordered even in the presence of FMN.

PubMed: 12798687
DOI: 10.1016/S0022-2836(03)00527-8

Experimental method

X-RAY DIFFRACTION (1.9 Å)