1W52
Crystal structure of a proteolyzed form of pancreatic lipase related protein 2 from horse
Summary for 1W52
| Entry DOI | 10.2210/pdb1w52/pdb |
| Descriptor | PANCREATIC LIPASE RELATED PROTEIN 2, DECYLAMINE-N,N-DIMETHYL-N-OXIDE, CALCIUM ION (3 entities in total) |
| Functional Keywords | lipase, pancreatic lipase related proteins, detergent, cleaved flap |
| Biological source | EQUUS CABALLUS (HORSE) |
| Total number of polymer chains | 1 |
| Total formula weight | 50597.69 |
| Authors | Mancheno, J.M.,Jayne, S.,Kerfelec, B.,Chapus, C.,Crenon, I.,Hermoso, J.A. (deposition date: 2004-08-04, release date: 2006-07-12, Last modification date: 2024-11-06) |
| Primary citation | Mancheno, J.M.,Jayne, S.,Kerfelec, B.,Chapus, C.,Crenon, I.,Hermoso, J.A. Crystalization of a Proteolyzed Form of the Horse Pancreatic Lipase-Related Protein 2: Structural Basis for the Specific Detergent Requirement. Acta Crystallogr.,Sect.D, 60:2107-, 2004 Cited by PubMed 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. PubMed: 15502342DOI: 10.1107/S0907444904024229 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.99 Å) |
Structure validation
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