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1W52

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

1W52 の概要
エントリーDOI10.2210/pdb1w52/pdb
分子名称PANCREATIC LIPASE RELATED PROTEIN 2, DECYLAMINE-N,N-DIMETHYL-N-OXIDE, CALCIUM ION (3 entities in total)
機能のキーワードlipase, pancreatic lipase related proteins, detergent, cleaved flap
由来する生物種EQUUS CABALLUS (HORSE)
タンパク質・核酸の鎖数1
化学式量合計50597.69
構造登録者
Mancheno, J.M.,Jayne, S.,Kerfelec, B.,Chapus, C.,Crenon, I.,Hermoso, J.A. (登録日: 2004-08-04, 公開日: 2006-07-12, 最終更新日: 2024-11-06)
主引用文献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: 15502342
DOI: 10.1107/S0907444904024229
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.99 Å)
構造検証レポート
Validation report summary of 1w52
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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