1GDN

FUSARIUM OXYSPORUM TRYPSIN AT ATOMIC RESOLUTION

1GDN の概要

• エントリーDOI: 10.2210/pdb1gdn/pdb
• 関連するPDBエントリー: 1fn8 1try
• 分子名称: TRYPSIN, GLY-ALA-LYS, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: beta barrel, hydrolase, hydrolase-hydrolase substrate complex, hydrolase/hydrolase substrate
• 由来する生物種: Fusarium oxysporum
• 細胞内の位置: Secreted: P35049
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22940.25

構造登録者

Rypniewski, W.R.,Oestergaard, P.,Noerregaard-Madsen, M.,Dauter, M.,Wilson, K.S. (登録日: 2000-09-28, 公開日: 2001-02-07, 最終更新日: 2024-11-06)

主引用文献

Rypniewski, W.R.,Ostergaard, P.R.,Norregaard-Madsen, M.,Dauter, M.,Wilson, K.S.
Fusarium oxysporum trypsin at atomic resolution at 100 and 283 K: a study of ligand binding.
Acta Crystallogr.,Sect.D, 57:8-19, 2001

PubMed Abstract: The X-ray structure of F. oxysporum trypsin has been determined at atomic resolution, revealing electron density in the binding site which was interpreted as a peptide bound in the sites S1, S2 and S3. The structure, which was initially determined at 1.07 A resolution and 283 K, has an Arg in the S1 specificity pocket. The study was extended to 0.81 A resolution at 100 K using crystals soaked in Arg, Lys and Gln to study in greater detail the binding at the S1 site. The electron density in the binding site was compared between the different structures and analysed in terms of partially occupied and overlapping components of peptide, solvent water and possibly other chemical moieties. Arg-soaked crystals reveal a density more detailed but similar to the original structure, with the Arg side chain visible in the S1 pocket and residual peptide density in the S2 and S3 sites. The density in the active site is complex and not fully interpreted. Lys at high concentrations displaces Arg in the S1 pocket, while some main-chain density remains in sites S2 and S3. Gln has been shown not to bind. The free peptide in the S1-S3 sites binds in a similar way to the binding loop of BPTI or the inhibitory domain of the Alzheimer's beta-protein precursor, with some differences in the S1 site.

PubMed: 11134922
DOI: 10.1107/S0907444900014116

実験手法

X-RAY DIFFRACTION (0.81 Å)