PDBsum entry: 1w52

Lipase

PDB id: 1w52

Contents

Protein chain

448 a.a. *

Ligands

DDQ ×2

Metals

_CA ×2

* Residue conservation analysis

PDB id:

1w52

Name:

Lipase

Title:

Crystal structure of a proteolyzed form of pancreatic lipase related protein 2 from horse

Structure:

Pancreatic lipase related protein 2. Chain: x

Source:

Equus caballus. Horse. Organism_taxid: 9796. Organ: pancreas

Resolution:

2.99Å R-factor: 0.234 R-free: 0.294

Authors:

J.M.Mancheno,S.Jayne,B.Kerfelec,C.Chapus,I.Crenon, J.A.Hermoso

Key ref:

J.M.Mancheño et al. (2004). Crystallization of a proteolyzed form of the horse pancreatic lipase-related protein 2: structural basis for the specific detergent requirement. Acta Crystallogr D Biol Crystallogr, 60, 2107-2109. PubMed id: 15502342 DOI: 10.1107/S0907444904024229

Date:

04-Aug-04 Release date: 12-Jul-06

Protein chain

Q95KP4  (Q95KP4_HORSE) -  Pancreatic lipase-related protein type 2 (Fragment)

Seq: 452 a.a.

Struc: 448 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular region (1 term)
• Biological process: lipid metabolic process (1 term)
• Biochemical function: catalytic activity (5 terms)

DOI no: 10.1107/S0907444904024229

Acta Crystallogr D Biol Crystallogr 60:2107-2109 (2004)

PubMed id: 15502342

Crystallization of a proteolyzed form of the horse pancreatic lipase-related protein 2: structural basis for the specific detergent requirement.

J.M.Mancheño, S.Jayne, B.Kerfelec, C.Chapus, I.Crenon, J.A.Hermoso.

ABSTRACT

Horse pancreatic lipase-related proteins PLRP1 and PLRP2 are produced by the pancreas together with pancreatic lipase (PL). Sequence-comparison analyses reveal that the three proteins possess the same two-domain organization: an N-terminal catalytic domain and a C-terminal domain, which in PL is involved in colipase binding. Nevertheless, despite the high level of sequence identity found, they exhibit distinct enzymatic properties. The intrinsic sensitivity of the peptide bond between Ser245 and Thr246 within the flap region of PLRP2 to proteolytic cleavage probably complicates PLRP2 crystallization since, as shown here, this proteolyzed form of PLRP2 is only crystallized after specific detergent stabilization of this region. This has been performed by the hanging-drop vapour-diffusion method at 291 K and exclusively in the presence of N,N-dimethyldecylamine-beta-oxide (DDAO). However, most crystals (>95%) are highly twinned and diffract poorly (to approximately 7-5 A resolution). Diffraction-quality trigonal crystals have unit-cell parameters a = b = 128.4, c = 85.8 A and belong to space group P3(2)21. A 2.9 A native data set was collected at ESRF on beamline ID14-2 with an R(merge) of 12.7%. Preliminary structural analysis provides a structural basis for the specific roles of DDAO.

Selected figure(s)

Figure 1.
Figure 1 Crystals of PLRP2 grown at 291 K in 28%(w/v) polyethylene glycol 6000, 0.1 M Tris-Gly pH 8.5 containing 20.8 mM N,N-dimethyldecylamine- -oxide (DDAO). The bar indicates 0.3 mm.

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 2107-2109) copyright 2004.

Figure was selected by an automated process.