1GPL

RP2 LIPASE

Summary for 1GPL

• Entry DOI: 10.2210/pdb1gpl/pdb
• Descriptor: RP2 LIPASE, CALCIUM ION (3 entities in total)
• Functional Keywords: serine esterase, hydrolase, lipid degradation, pancreas, glycoprotein, chimeric
• Biological source: Cavia porcellus (domestic guinea pig)
• Cellular location: Secreted: P16233
• Total number of polymer chains: 1
• Total formula weight: 47915.92

Authors

Withers-Martinez, C.,Cambillau, C. (deposition date: 1996-07-13, release date: 1997-02-12, Last modification date: 2024-11-13)

Primary citation

Withers-Martinez, C.,Carriere, F.,Verger, R.,Bourgeois, D.,Cambillau, C.
A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig.
Structure, 4:1363-1374, 1996

PubMed Abstract: The guinea pig pancreatic lipase-related protein 2 (GPLRP2) differs from classical pancreatic lipases in that it displays both lipase and phospholipase A1 activities; classical pancreatic lipases have no phospholipase activity. The sequence of GPLRP2 is 63 % identical to that of human pancreatic lipase (HPL), but the so-called lid domain, is much reduced in GPLRP2. A phospholipase A1 from hornet venom (Dolml PLA1) is very similar to HPL and GPLRP2 but is devoid of lipase activity; Dolml PLA1 also contains a reduced lid domain and lacks a region termed the beta9 loop, which is located in the vicinity of the HPL and GPLRP2 active sites. The structure determination of a chimera of GPLRP2 and HPL and domain building of Dolml PLA1 were undertaken to gain a better understanding of the structural parameters responsible for the differences in lipase versus phospholipase activity among these structurally related enzymes.

PubMed: 8939760
DOI: 10.1016/S0969-2126(96)00143-8

Experimental method

X-RAY DIFFRACTION (2.01 Å)