PDBsum entry 1rp1

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Hydrolase PDB id
Jmol PyMol
Protein chain
441 a.a. *
Waters ×358
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Dog pancreatic lipase related protein 1
Structure: Pancreatic lipase related protein 1. Chain: a. Ec:
Source: Canis lupus familiaris. Dog. Organism_taxid: 9615. Strain: familiaris. Organ: pancreas. Secretion: pancreatic juice
2.10Å     R-factor:   0.195     R-free:   0.256
Authors: A.Roussel,C.Cambillau
Key ref: A.Roussel et al. (1998). Reactivation of the totally inactive pancreatic lipase RP1 by structure-predicted point mutations. Proteins, 32, 523-531. PubMed id: 9726421
02-Apr-98     Release date:   17-Jun-98    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P06857  (LIPR1_CANFA) -  Inactive pancreatic lipase-related protein 1
467 a.a.
441 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - Triacylglycerol lipase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Triacylglycerol + H2O = diacylglycerol + a carboxylate
+ H(2)O
= diacylglycerol
+ carboxylate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     lipid metabolic process   2 terms 
  Biochemical function     carboxylic ester hydrolase activity     5 terms  


Proteins 32:523-531 (1998)
PubMed id: 9726421  
Reactivation of the totally inactive pancreatic lipase RP1 by structure-predicted point mutations.
A.Roussel, Caro, S.Bezzine, L.Gastinel, Caro, F.Carrière, S.Leydier, R.Verger, C.Cambillau.
Both classical pancreatic lipase (DPL) and pancreatic lipase-related protein 1 (DPLRP1) have been found to be secreted by dog exocrine pancreas. These two proteins were purified to homogeneity from canine pancreatic juice and no significant catalytic activity was observed with dog PLRP1 on any of the substrates tested: di- and tri-glycerides, phospholipids, etc. DPLRP1 was crystallized and its structure solved by molecular replacement and refined at a resolution of 2.10 A. Its structure is similar to that of the classical PL structures in the absence of any inhibitors or micelles. The lid domain that controls the access to the active site was found to have a closed conformation. An amino-acid substitution (Ala 178 Val) in the DPLRP1 may result in a steric clash with one of the acyl chains observed in the structures of a C11 alkyl phosphonate inhibitor, a transition state analogue, bound to the classical PL. This substitution was suspected of being responsible for the absence of DPLRP1 activity. The presence of Val and Ala residues in positions 178 and 180, respectively, are characteristic of all the known PLRP1, whereas Ala and Pro residues are always present in the same positions in all the other members of the PL gene family. Introducing the double mutation Val 178 Ala and Ala 180 Pro into the human pancreatic RP1 (HPLRP1) gene yielded a well expressed and folded enzyme in insect cells. This enzyme is kinetically active on triglycerides. Our findings on DPLRP1 and HPLRP1 are therefore likely to apply to all the RP1 lipases.

Literature references that cite this PDB file's key reference

  PubMed id Reference
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.  
15890938 J.P.Kamil, B.K.Tischer, S.Trapp, V.K.Nair, N.Osterrieder, and H.J.Kung (2005).
vLIP, a viral lipase homologue, is a virulence factor of Marek's disease virus.
  J Virol, 79, 6984-6996.  
15181189 R.Z.Birk, K.S.Regan, E.Boyle-Roden, and P.M.Brannon (2004).
Pancreatic lipase and its related protein 2 are regulated by dietary polyunsaturated fat during the postnatal development of rats.
  Pediatr Res, 56, 256-262.  
10358049 A.Roussel, S.Canaan, M.P.Egloff, M.Rivière, L.Dupuis, R.Verger, and C.Cambillau (1999).
Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest.
  J Biol Chem, 274, 16995-17002.
PDB code: 1hlg
10570246 S.Longhi, and C.Cambillau (1999).
Structure-activity of cutinase, a small lipolytic enzyme.
  Biochim Biophys Acta, 1441, 185-196.  
9822688 A.Roussel, Y.Yang, F.Ferrato, R.Verger, C.Cambillau, and M.Lowe (1998).
Structure and activity of rat pancreatic lipase-related protein 2.
  J Biol Chem, 273, 32121-32128.
PDB code: 1bu8
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