4L7Z

Crystal Structure of Chloroflexus aurantiacus malyl-CoA lyase

4L7Z の概要

• エントリーDOI: 10.2210/pdb4l7z/pdb
• 関連するPDBエントリー: 4L80 4L9Y 4L9Z
• 分子名称: HpcH/HpaI aldolase, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
• 機能のキーワード: tim barrel, lyase
• 由来する生物種: Chloroflexus aurantiacus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 230736.35

構造登録者

Zarzycki, J.,Kerfeld, C.A. (登録日: 2013-06-14, 公開日: 2013-12-04, 最終更新日: 2023-09-20)

主引用文献

Zarzycki, J.,Kerfeld, C.A.
The crystal structures of the tri-functional Chloroflexus aurantiacus and bi-functional Rhodobacter sphaeroides malyl-CoA lyases and comparison with CitE-like superfamily enzymes and malate synthases.
Bmc Struct.Biol., 13:28-28, 2013

PubMed Abstract: Malyl-CoA lyase (MCL) is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related Coenzyme A (CoA) thioesters. This enzyme plays a crucial, multifunctional role in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation in Chloroflexus aurantiacus. A second, phylogenetically distinct MCL from Rhodobacter sphaeroides is involved in the ethylmalonyl-CoA pathway for acetate assimilation. Both MCLs belong to the large superfamily of CitE-like enzymes, which includes the name-giving β-subunit of citrate lyase (CitE), malyl-CoA thioesterases and other enzymes of unknown physiological function. The CitE-like enzyme superfamily also bears sequence and structural resemblance to the malate synthases. All of these different enzymes share highly conserved catalytic residues, although they catalyze distinctly different reactions: C-C bond formation and cleavage, thioester hydrolysis, or both (the malate synthases).

PubMed: 24206647
DOI: 10.1186/1472-6807-13-28

実験手法

X-RAY DIFFRACTION (2.502 Å)