1F75

CRYSTAL STRUCTURE OF UNDECAPRENYL DIPHOSPHATE SYNTHASE FROM MICROCOCCUS LUTEUS B-P 26

1F75 の概要

• エントリーDOI: 10.2210/pdb1f75/pdb
• 分子名称: UNDECAPRENYL PYROPHOSPHATE SYNTHETASE, SULFATE ION (3 entities in total)
• 機能のキーワード: parallel beta sheet, new fold for isoprenoid synthase, peptidoglycan synthesis, transferase
• 由来する生物種: Micrococcus luteus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58082.58

構造登録者

Fujihashi, M.,Zhang, Y.-W.,Higuchi, Y.,Li, X.-Y.,Koyama, T.,Miki, K. (登録日: 2000-06-26, 公開日: 2001-03-28, 最終更新日: 2024-02-07)

主引用文献

Fujihashi, M.,Zhang, Y.W.,Higuchi, Y.,Li, X.Y.,Koyama, T.,Miki, K.
Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase.
Proc.Natl.Acad.Sci.USA, 98:4337-4342, 2001

PubMed Abstract: Undecaprenyl diphosphate synthase (UPS) catalyzes the cis-prenyl chain elongation onto trans, trans-farnesyl diphosphate (FPP) to produce undecaprenyl diphosphate (UPP), which is indispensable for the biosynthesis of bacterial cell walls. We report here the crystal structure of UPS as the only three-dimensional structure among cis-prenyl chain elongating enzymes. The structure is classified into a protein fold family and is completely different from the so-called "isoprenoid synthase fold" that is believed to be a common structure for the enzymes relating to isoprenoid biosynthesis. Conserved amino acid residues among cis-prenyl chain elongating enzymes are located around a large hydrophobic cleft in the UPS structure. A structural P-loop motif, which frequently appears in the various kinds of phosphate binding site, is found at the entrance of this cleft. The catalytic site is determined on the basis of these structural features, from which a possible reaction mechanism is proposed.

PubMed: 11287651
DOI: 10.1073/pnas.071514398

実験手法

X-RAY DIFFRACTION (2.2 Å)