1R67

Y104A MUTANT OF E.COLI IPP ISOMERASE

Summary for 1R67

• Entry DOI: 10.2210/pdb1r67/pdb
• Related: 1HX3 1HZT 1N2U 1PVU
• Descriptor: Isopentenyl-diphosphate delta-isomerase, MAGNESIUM ION (3 entities in total)
• Functional Keywords: complex y104a mutant, isomerase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: Q46822
• Total number of polymer chains: 1
• Total formula weight: 21534.59

Authors

Wouters, J. (deposition date: 2003-10-15, release date: 2003-10-21, Last modification date: 2023-08-23)

Primary citation

de Ruyck, J.,Durisotti, V.,Oudjama, Y.,Wouters, J.
Structural role for Tyr-104 in Escherichia coli isopentenyl-diphosphate isomerase: site-directed mutagenesis, enzymology, and protein crystallography.
J.Biol.Chem., 281:17864-17869, 2006

PubMed Abstract: Isopentenyl-diphosphate (IPP):dimethylallyl diphosphate isomerase is a key enzyme in the biosynthesis of isoprenoids. The mechanism of the isomerization reaction involves protonation of the unactivated carbon-carbon double bond in the substrate, but identity of the acidic moiety providing the proton is still not clear. Multiple sequence alignments and geometrical features observed in crystal structures of complexes with IPP isomerase suggest that Tyr-104 could play an important role during catalysis. A series of mutants was constructed by directed mutagenesis and characterized by enzymology. Crystallographic and thermal denaturation data for Y104A and Y104F mutants were obtained. Those data demonstrate the importance of residue Tyr-104 for proper folding of Escherichia coli type I IPP isomerase.

PubMed: 16617181
DOI: 10.1074/jbc.M601851200

Experimental method

X-RAY DIFFRACTION (1.77 Å)