1C8B

CRYSTAL STRUCTURE OF A NOVEL GERMINATION PROTEASE FROM SPORES OF BACILLUS MEGATERIUM: STRUCTURAL REARRANGEMENTS AND ZYMOGEN ACTIVATION

1C8B の概要

• エントリーDOI: 10.2210/pdb1c8b/pdb
• 分子名称: SPORE PROTEASE (2 entities in total)
• 機能のキーワード: novel fold, hydrolase
• 由来する生物種: Bacillus megaterium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81346.52

構造登録者

Ponnuraj, K.,Rowland, S.,Nessi, C.,Setlow, P.,Jedrzejas, M.J. (登録日: 2000-05-03, 公開日: 2001-05-03, 最終更新日: 2023-12-27)

主引用文献

Ponnuraj, K.,Rowland, S.,Nessi, C.,Setlow, P.,Jedrzejas, M.J.
Crystal structure of a novel germination protease from spores of Bacillus megaterium: structural arrangement and zymogen activation.
J.Mol.Biol., 300:1-10, 2000

PubMed Abstract: The DNA in the core of spores of Bacillus species is saturated with a group of small, acid-soluble proteins (SASP) that protect DNA from a variety of harsh treatments and play a major role in spore resistance and long-term spore survival. During spore germination, SASPs are rapidly degraded to amino acids and this degradation is initiated by a sequence-specific protease called germination protease (GPR), which exhibits no obvious mechanistic or amino acid sequence similarity to any known class of proteases. GPR is synthesized during sporulation as an inactive tetrameric zymogen termed P(46), which later autoprocesses to a smaller form termed P(41), which is active only during spore germination. Here, we report the crystal structure of P(46) from Bacillus megaterium at 3.0 A resolution and the fact that P(46) monomer adopts a novel fold. The asymmetric unit contains two P(46) monomers and the functional tetramer is a dimer of dimers, with an approximately 9 A channel in the center of the tetramer. Analysis of the P(46) structure and site-directed mutagenesis studies have provided some insight into the mechanism of zymogen activation as well as the zymogen's lack of activity and the inactivity of P(41) in the mature spore.

PubMed: 10864493
DOI: 10.1006/jmbi.2000.3849

実験手法

X-RAY DIFFRACTION (3 Å)