PDBsum entry 1bu8

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protein ligands links
Hydrolase PDB id
Jmol PyMol
Protein chain
446 a.a. *
Waters ×295
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Rat pancreatic lipase related protein 2
Structure: Protein (pancreatic lipase related protein 2). Chain: a. Engineered: yes
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Organ: pancreas. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
1.80Å     R-factor:   0.202     R-free:   0.244
Authors: A.Roussel,C.Cambillau
Key ref:
A.Roussel et al. (1998). Structure and activity of rat pancreatic lipase-related protein 2. J Biol Chem, 273, 32121-32128. PubMed id: 9822688 DOI: 10.1074/jbc.273.48.32121
14-Sep-98     Release date:   23-Dec-98    
Go to PROCHECK summary

Protein chain
-  (POLG_HAVHM) - 
Protein chain
Pfam   ArchSchema ?
P54318  (LIPR2_RAT) -  Pancreatic lipase-related protein 2
468 a.a.
446 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 1: E.C.  - Galactolipase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + 2 H2O = 3-beta-D- galactosyl-sn-glycerol + 2 carboxylates
+ 2 × H(2)O
= 3-beta-D- galactosyl-sn-glycerol
Bound ligand (Het Group name = NAG)
matches with 47.62% similarity
+ 2 × carboxylates
   Enzyme class 2: E.C.  - Triacylglycerol lipase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Triacylglycerol + H2O = diacylglycerol + a carboxylate
+ 2 × H(2)O
= diacylglycerol
+ 2 × carboxylate
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   4 terms 
  Biological process     post-embryonic development   9 terms 
  Biochemical function     carboxylic ester hydrolase activity     10 terms  


DOI no: 10.1074/jbc.273.48.32121 J Biol Chem 273:32121-32128 (1998)
PubMed id: 9822688  
Structure and activity of rat pancreatic lipase-related protein 2.
A.Roussel, Y.Yang, F.Ferrato, R.Verger, C.Cambillau, M.Lowe.
The pancreas expresses several members of the lipase gene family including pancreatic triglyceride lipase (PTL) and two homologous proteins, pancreatic lipase-related proteins 1 and 2 (PLRP1 and PLRP2). Despite their similar amino acid sequences, PTL, PLRP1, and PLRP2 differ in important kinetic properties. PLRP1 has no known activity. PTL and PLRP2 differ in substrate specificity, bile acid inhibition, colipase requirement, and interfacial activation. To begin understanding the structural explanations for these functional differences, we solved the crystal structure of rat (r)PLRP2 and further characterized its kinetic properties. The 1.8 A structure of rPLRP2, like the tertiary structure of human PTL, has a globular N-terminal domain and a beta-sandwich C-terminal domain. The lid domain occupied the closed position, suggesting that rPLRP2 should show interfacial activation. When we reexamined this issue with tripropionin as substrate, rPLRP2 exhibited interfacial activation. Because the active site topology of rPLRP2 resembled that of human PTL, we predicted and demonstrated that the lipase inhibitors E600 and tetrahydrolipstatin inhibit rPLRP2. Although PTL and rPLRP2 have similar active sites, rPLRP2 has a broader substrate specificity that we confirmed using a monolayer technique. With this assay, we showed for the first time that rPLRP2 prefers phosphatidylglycerol and ethanolamine over phosphatidylcholine. In summary, we confirmed and extended the observation that PLRP2 lipases have a broader substrate specificity than PTL, we demonstrated that PLRP2 lipases show interfacial activation, and we solved the first crystal structure of a PLRP2 lipase that contains a lid domain.
  Selected figure(s)  
Figure 1.
Fig. 1. Stereo view of the sigma weighted electron density map of the closed lid contoured a 1 .
Figure 2.
Fig. 2. Structure of rPLRP2. A, stereo view of the C trace of rPLRP2. The side chains of the N and C terminus residues as well as those of the catalytic Ser152 and of the lid residue Trp252 are represented. The ethylene glycol molecules (blue) and the GlcNAc residue linked to Asn334 are shown. Green, C terminus domain; brown, N-terminal catalytic domain; yellow, catalytic domain following the lid; pink, lid. B, stereo view of the C trace of rPLRP2 superimposed on those of the other known closed pancreatic lipase structures.
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (1998, 273, 32121-32128) copyright 1998.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20179589 S.Lindquist, and O.Hernell (2010).
Lipid digestion and absorption in early life: an update.
  Curr Opin Clin Nutr Metab Care, 13, 314-320.  
19346257 A.Bourbon-Freie, R.E.Dub, X.Xiao, and M.E.Lowe (2009).
Trp-107 and trp-253 account for the increased steady state fluorescence that accompanies the conformational change in human pancreatic triglyceride lipase induced by tetrahydrolipstatin and bile salt.
  J Biol Chem, 284, 14157-14164.  
19325035 B.Alves, J.Leong, D.L.Tamang, V.Elliott, M.Lowe, and D.Hudig (2009).
Hydrolysis of tumor cell lipids after CTL-mediated death.
  Int Immunol, 21, 543-553.  
19451396 B.N.Alves, J.Leong, D.L.Tamang, V.Elliott, J.Edelnant, D.Redelman, C.A.Singer, A.R.Kuhn, R.Miller, M.E.Lowe, and D.Hudig (2009).
Pancreatic lipase-related protein 2 (PLRP2) induction by IL-4 in cytotoxic T lymphocytes (CTLs) and reevaluation of the negative effects of its gene ablation on cytotoxicity.
  J Leukoc Biol, 86, 701-712.  
17961181 A.Berton, C.Sebban-Kreuzer, and I.Crenon (2007).
Role of the structural domains in the functional properties of pancreatic lipase-related protein 2.
  FEBS J, 274, 6011-6023.  
17205399 D.C.Whitcomb, and M.E.Lowe (2007).
Human pancreatic digestive enzymes.
  Dig Dis Sci, 52, 1.  
17805199 X.Li, S.Lindquist, M.Lowe, L.Noppa, and O.Hernell (2007).
Bile salt-stimulated lipase and pancreatic lipase-related protein 2 are the dominating lipases in neonatal fat digestion in mice and rats.
  Pediatr Res, 62, 537-541.  
15502342 J.M.Mancheño, S.Jayne, B.Kerfelec, C.Chapus, I.Crenon, and J.A.Hermoso (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.
PDB code: 1w52
12354219 C.Claudianos, J.T.Dessens, H.E.Trueman, M.Arai, J.Mendoza, G.A.Butcher, T.Crompton, and R.E.Sinden (2002).
A malaria scavenger receptor-like protein essential for parasite development.
  Mol Microbiol, 45, 1473-1484.  
12081491 S.Jayne, B.Kerfelec, E.Foglizzo, S.Granon, J.Hermoso, C.Chapus, and I.Crenon (2002).
Activation of horse PLRP2 by bile salts does not require colipase.
  Biochemistry, 41, 8422-8428.  
11746691 A.Henriksen, T.P.King, O.Mirza, R.I.Monsalve, K.Meno, H.Ipsen, J.N.Larsen, M.Gajhede, and M.D.Spangfort (2001).
Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily.
  Proteins, 45, 438-448.
PDB code: 1qnx
10674344 Y.Yang, D.Sanchez, C.Figarella, and M.E.Lowe (2000).
Discoordinate expression of pancreatic lipase and two related proteins in the human fetal pancreas.
  Pediatr Res, 47, 184-188.  
10570245 H.van Tilbeurgh, S.Bezzine, C.Cambillau, R.Verger, and F.Carrière (1999).
Colipase: structure and interaction with pancreatic lipase.
  Biochim Biophys Acta, 1441, 173-184.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.