4L80

Crystal Structure of Chloroflexus aurantiacus malyl-CoA lyase in complex with magnesium, oxalate, and propionyl-CoA

Summary for 4L80

• Entry DOI: 10.2210/pdb4l80/pdb
• Related: 4L7Z 4L9Y 4L9Z
• Descriptor: HpcH/HpaI aldolase, propionyl Coenzyme A, OXALATE ION, ... (6 entities in total)
• Functional Keywords: tim barrel, lyase
• Biological source: Chloroflexus aurantiacus
• Total number of polymer chains: 6
• Total formula weight: 236351.88

Authors

Zarzycki, J.,Kerfeld, C.A. (deposition date: 2013-06-15, release date: 2013-12-04, Last modification date: 2023-09-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.008 Å)