1ELT

STRUCTURE OF NATIVE PANCREATIC ELASTASE FROM NORTH ATLANTIC SALMON AT 1.61 ANGSTROMS RESOLUTION

1ELT の概要

• エントリーDOI: 10.2210/pdb1elt/pdb
• 分子名称: ELASTASE, CALCIUM ION (3 entities in total)
• 機能のキーワード: serine proteinase
• 由来する生物種: Salmo salar (Atlantic salmon)
• 細胞内の位置: Secreted : Q7SIG3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25073.96

構造登録者

Berglund, G.I.,Smalaas, A.O. (登録日: 1995-01-02, 公開日: 1996-01-01, 最終更新日: 2024-11-20)

主引用文献

Berglund, G.I.,Willassen, N.P.,Hordvik, A.,Smalas, A.O.
Structure of native pancreatic elastase from North Atlantic salmon at 1.61 A resolution.
Acta Crystallogr.,Sect.D, 51:925-937, 1995

PubMed Abstract: The crystal structure of native salmon pancreatic elastase (SPE) has been solved by molecular-replacement methods, and refined by conventional conjugate-gradient methods and simulated-annealing techniques. The final R value is 17.2% for 21 389 reflections between 8.0 and 1.61 A, and the corresponding free R value is 23.9%. The overall tertiary structure of SPE is remarkably similar to that of porcine pancreatic elastase I (PPE), to which it shows about 67% sequence identity. The primary structure of SPE is determined from the electron-density maps, and only about 15 side chains are somewhat uncertain. Interesting differences between SPE and PPE, are one sequence deletion assigned to position 186, the residue 192 at the entrance of the specificity pocket is substituted from a Gln in PPE to Asn in SPE, and one of the calcium ligands is different. Furthermore, electron density is missing in SPE for the last three residues of the C-terminal helix. A comparison of the present amino-acid sequence of SPE with other sequences available indicates that SPE belongs to the class 1 pancreatic elastases.

PubMed: 15299762
DOI: 10.1107/S0907444995004835

実験手法

X-RAY DIFFRACTION (1.61 Å)