1LDC

X-RAY STRUCTURE OF TWO COMPLEXES OF THE Y143F FLAVOCYTOCHROME B2 MUTANT CRYSTALLIZED IN THE PRESENCE OF LACTATE OR PHENYL-LACTATE

1LDC の概要

• エントリーDOI: 10.2210/pdb1ldc/pdb
• 分子名称: L-LACTATE DEHYDROGENASE, FLAVIN MONONUCLEOTIDE, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• 機能のキーワード: flavoenzyme, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Mitochondrion intermembrane space: P00175
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 115001.09

構造登録者

Tegoni, M.,Cambillau, C. (登録日: 1995-04-13, 公開日: 1995-07-10, 最終更新日: 2023-11-15)

主引用文献

Tegoni, M.,Begotti, S.,Cambillau, C.
X-ray structure of two complexes of the Y143F flavocytochrome b2 mutant crystallized in the presence of lactate or phenyl lactate.
Biochemistry, 34:9840-9850, 1995

PubMed Abstract: Flavocytochrome b2 is a flavohemo enzyme localized in the intermembrane space of yeast mitochondria, where it catalyzes the electron transfer from its substrate, L-lactate, to cytochrome c. We have obtained crystals of a flavocytochrome b2 mutant, Y143F, which are isostructural with those of the native recombinant enzyme [Tegoni, M., & Cambillau, C. (1994) Protein Sci.3, 303-314]. These crystals were grown under similar conditions to those used to obtain the recombinant enzyme, but in the presence of phenyl lactate or lactate. We report here on the structural analysis of the two complexes of flavocytochrome b2 with the reaction products at 2.9 A resolution. In both structures, the Phe143 phenyl ring keeps the same position as that of the phenolic ring of Tyr143 in both the native recombinant and in the native wild-type enzymes. The product of the reaction, phenyl pyruvate or pyruvate, is present at the active site of both subunits, and not only in subunit 2 as observed in the wild-type structure [Xia, Z.-X., & Mathews, F.S. (1990) J. Mol. Biol. 212, 837-863]. The number of interactions between the FMN and the heme domain is considerably lower in the Y143F mutant than in the native proteins. The latter finding strongly supports the hypothesis that the main role of Tyr143 in the native proteins. The latter findings strongly supports the hypothesis that the main role of Tyr143 in the native protein probably consists in establishing a hydrogen bond with the heme [Xia, Z.-X., & Mathews, F.S. (1990) J. Mol. Biol. 212, 837-863]. This interaction appears to be essential for the two domains to approach each other suitably so that the intramolecular electron transfer can occur.

PubMed: 7632684
DOI: 10.1021/bi00031a004

実験手法

X-RAY DIFFRACTION (2.9 Å)