1FI4

THE X-RAY CRYSTAL STRUCTURE OF MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AT 2.3 ANGSTROM RESOLUTION.

1FI4 の概要

• エントリーDOI: 10.2210/pdb1fi4/pdb
• 分子名称: MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE (2 entities in total)
• 機能のキーワード: mixed alpha/beta structure, atp binding, decarboxylase, cholesterol biosynthesis, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, lyase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46804.04

構造登録者

Bonanno, J.B.,Edo, C.,Eswar, N.,Pieper, U.,Romanowski, M.J.,Ilyin, V.,Gerchman, S.E.,Kycia, H.,Studier, F.W.,Sali, A.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2000-08-03, 公開日: 2001-03-21, 最終更新日: 2024-10-16)

主引用文献

Bonanno, J.B.,Edo, C.,Eswar, N.,Pieper, U.,Romanowski, M.J.,Ilyin, V.,Gerchman, S.E.,Kycia, H.,Studier, F.W.,Sali, A.,Burley, S.K.
Structural genomics of enzymes involved in sterol/isoprenoid biosynthesis.
Proc.Natl.Acad.Sci.USA, 98:12896-12901, 2001

PubMed Abstract: X-ray structures of two enzymes in the sterol/isoprenoid biosynthesis pathway have been determined in a structural genomics pilot study. Mevalonate-5-diphosphate decarboxylase (MDD) is a single-domain alpha/beta protein that catalyzes the last of three sequential ATP-dependent reactions which convert mevalonate to isopentenyl diphosphate. Isopentenyl disphosphate isomerase (IDI) is an alpha/beta metalloenzyme that catalyzes interconversion of isopentenyl diphosphate and dimethylallyl diphosphate, which condense in the next step toward synthesis of sterols and a host of natural products. Homology modeling of related proteins and comparisons of the MDD and IDI structures with two other experimentally determined structures have shown that MDD is a member of the GHMP superfamily of small-molecule kinases and IDI is similar to the nudix hydrolases, which act on nucleotide diphosphatecontaining substrates. Structural models were produced for 379 proteins, encompassing a substantial fraction of both protein superfamilies. All three enzymes responsible for synthesis of isopentenyl diphosphate from mevalonate (mevalonate kinase, phosphomevalonate kinase, and MDD) share the same fold, catalyze phosphorylation of chemically similar substrates (MDD decarboxylation involves phosphorylation of mevalonate diphosphate), and seem to have evolved from a common ancestor. These structures and the structural models derived from them provide a framework for interpreting biochemical function and evolutionary relationships.

PubMed: 11698677
DOI: 10.1073/pnas.181466998

実験手法

X-RAY DIFFRACTION (2.27 Å)