6OWE

Enoyl-CoA carboxylases/reductases in complex with ethylmalonyl CoA

6OWE の概要

• エントリーDOI: 10.2210/pdb6owe/pdb
• 分子名称: Crotonyl-CoA carboxylase/reductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 5'-O-[(S)-{[(S)-[(3R)-4-({(1E)-3-[(2-{[(2S)-2-carboxybutanoyl]sulfanyl}ethyl)amino]-3-oxoprop-1-en-1-yl}amino)-3-hydroxy-2,2-dimethyl-4-oxobutoxy](hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]adenosine 3'-(dihydrogen phosphate), ... (5 entities in total)
• 機能のキーワード: ecr, highly efficient co2-fixing enzyme, oxidoreductase
• 由来する生物種: Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 / KM-6054)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 201907.07

構造登録者

DeMirci, H. (登録日: 2019-05-09, 公開日: 2019-06-26, 最終更新日: 2024-03-13)

主引用文献

Stoffel, G.M.M.,Saez, D.A.,DeMirci, H.,Vogeli, B.,Rao, Y.,Zarzycki, J.,Yoshikuni, Y.,Wakatsuki, S.,Vohringer-Martinez, E.,Erb, T.J.
Four amino acids define the CO2binding pocket of enoyl-CoA carboxylases/reductases.
Proc.Natl.Acad.Sci.USA, 116:13964-13969, 2019

PubMed Abstract: Carboxylases are biocatalysts that capture and convert carbon dioxide (CO) under mild conditions and atmospheric concentrations at a scale of more than 400 Gt annually. However, how these enzymes bind and control the gaseous CO molecule during catalysis is only poorly understood. One of the most efficient classes of carboxylating enzymes are enoyl-CoA carboxylases/reductases (Ecrs), which outcompete the plant enzyme RuBisCO in catalytic efficiency and fidelity by more than an order of magnitude. Here we investigated the interactions of CO within the active site of Ecr from Combining experimental biochemistry, protein crystallography, and advanced computer simulations we show that 4 amino acids, N81, F170, E171, and H365, are required to create a highly efficient CO-fixing enzyme. Together, these 4 residues anchor and position the CO molecule for the attack by a reactive enolate created during the catalytic cycle. Notably, a highly ordered water molecule plays an important role in an active site that is otherwise carefully shielded from water, which is detrimental to CO fixation. Altogether, our study reveals unprecedented molecular details of selective CO binding and C-C-bond formation during the catalytic cycle of nature's most efficient CO-fixing enzyme. This knowledge provides the basis for the future development of catalytic frameworks for the capture and conversion of CO in biology and chemistry.

PubMed: 31243147
DOI: 10.1073/pnas.1901471116

実験手法

X-RAY DIFFRACTION (1.72 Å)