Crystal structure of type 2 isopentenyl diphosphate isomerase from Thermus thermophilus in complex with inorganic pyrophosphate

Jérôme De Ruyck, Jenny Pouyez, Steven C. Rothman, Dale Poulter, Johan Wouters

Research output: Contribution to journalArticlepeer-review

Abstract

The N-terminal region is stabilized in the crystal structure of Thermus thermophilus type 2 isopentenyl diphosphate isomerase in complex with inorganic pyrophosphate, providing new insights about the active site and the catalytic mechanism of the enzyme. The PPi moiety is located near the conserved residues, H10, R97, H152, Q157, E158, and W219, and the flavin cofactor. The putative active site of isopentenyl diphosphate isomerase 2 provides interactions for stabilizing a carbocationic intermediate similar to those that stabilize the intermediate in the well-established protonation-deprotonation mechanism of isopentenyl diphosphate isomerase 1.

Original languageEnglish
Pages (from-to)9051-9053
Number of pages3
JournalBiochemistry
Volume47
Issue number35
DOIs
Publication statusPublished - 2 Sep 2008

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