PDBsum entry: 1fxw

Hydrolase

PDB id: 1fxw

Contents

Protein chains

211 a.a. *

212 a.a. *

Metals

_CA

Waters ×121

* Residue conservation analysis

PDB id:

1fxw

Name:

Hydrolase

Title:

Crystal structure of the recombinant alpha1/alpha2 catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase ib.

Structure:

Platelet-activating factor acetylhydrolase ib gamma subunit. Chain: a. Synonym: alpha1. Engineered: yes. Platelet-activating factor acetylhydrolase ib beta subunit. Chain: f. Synonym: alpha2.

Source:

Bos taurus. Cattle. Organism_taxid: 9913. Organ: brain. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

2.10Å R-factor: 0.212 R-free: 0.275

Authors:

Z.Derewenda,J.Li

Key ref:

P.J.Sheffield et al. (2001). Preparation and crystal structure of the recombinant alpha(1)/alpha(2) catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase Ib. Protein Eng, 14, 513-519. PubMed id: 11522926 DOI: 10.1093/protein/14.7.513

Date:

27-Sep-00 Release date: 12-Dec-01

Protein chain

Q29460  (PA1B3_BOVIN) -  Platelet-activating factor acetylhydrolase IB subunit gamma

Seq: 232 a.a.

Struc: 211 a.a.

Protein chain

P68401  (PA1B2_BOVIN) -  Platelet-activating factor acetylhydrolase IB subunit beta

Seq: 229 a.a.

Struc: 212 a.a.

Enzyme reactions

• Enzyme class: Chains A, F: E.C.3.1.1.47 - 1-alkyl-2-acetylglycerophosphocholine esterase.
• Reaction: 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H₂O = 1-alkyl- sn-glycero-3-phosphocholine + acetate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: cytoplasm (1 term)
• Biological process: lipid metabolic process (3 terms)
• Biochemical function: protein binding (4 terms)

Added reference

DOI no: 10.1093/protein/14.7.513

Protein Eng 14:513-519 (2001)

PubMed id: 11522926

Preparation and crystal structure of the recombinant alpha(1)/alpha(2) catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase Ib.

P.J.Sheffield, T.W.McMullen, J.Li, Y.S.Ho, S.M.Garrard, U.Derewenda, Z.S.Derewenda.

ABSTRACT

The intracellular form of mammalian platelet activating factor acetylhydrolase found in brain (PAF-AH Ib) is thought to play a critical role in control in neuronal migration during cortex development. This oligomeric complex consists of a homodimer of the 45 kDa (beta) LIS1 protein, the product of the causative gene for type I lissencephaly, and, depending on the developmental stage and species, one of three possible pairs of two homologous approximately 26 kDa alpha-subunits, which harbor all of the catalytic activity. The exact composition of this complex depends on the expression patterns of the alpha(1) and alpha(2) genes, exhibiting tissue specificity and developmental control. All three possible dimers (alpha(1)/alpha(1), alpha(1)/alpha(2) and alpha(2)/alpha(2)) were identified in tissues. The alpha(1)/alpha(2) heterodimer is thought to play an important role in fetal brain. The structure of the alpha(1)/alpha(1) homodimer was solved earlier in our laboratory at 1.7 A. We report here the preparation of recombinant alpha(1)/alpha(2) heterodimers using a specially constructed bi-cistronic expression vector. The approach may be useful in studies of other systems where pure heterodimers of recombinant proteins are required. The alpha(1)/alpha(2) dimer has been crystallized and its structure was solved at 2.1 A resolution by molecular replacement. These results set the stage for a detailed characterization of the PAF-AH Ib complex.