2ftp

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Crystal Structure of hydroxymethylglutaryl-CoA lyase from Pseudomonas aeruginosa

Structural highlights

2ftp is a 1 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:GOL, NA
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

LIUE_PSEAE Involved in the L-leucine, isovalerate and acyclic monoterpene catabolism. Catalyzes the cleavage of 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to yield acetyl-CoA and acetoacetate. It can also catalyze the cleavage of 3-hydroxy-3-isohexenylglutaryl-CoA (HIHG_CoA) to yield 7-methyl-3-oxooct-6-enoyl-CoA and acetate.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. Chávez-Avilés M, Díaz-Pérez AL, Reyes-de la Cruz H, Campos-García J. The Pseudomonas aeruginosa liuE gene encodes the 3-hydroxy-3-methylglutaryl coenzyme A lyase, involved in leucine and acyclic terpene catabolism. FEMS Microbiol Lett. 2009 Jul;296(1):117-23. PMID:19459965 doi:10.1111/j.1574-6968.2009.01624.x
  2. Chávez-Avilés M, Díaz-Pérez AL, Campos-García J. The bifunctional role of LiuE from Pseudomonas aeruginosa, displays additionally HIHG-CoA lyase enzymatic activity. Mol Biol Rep. 2010 Apr;37(4):1787-91. PMID:19597963 doi:10.1007/s11033-009-9611-6

Contents


PDB ID 2ftp

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