3HBV

PrtC methionine mutants: M226A in-house

3HBV の概要

• エントリーDOI: 10.2210/pdb3hbv/pdb
• 関連するPDBエントリー: 1GO7 1GO8 1K7G 3HB2 3HBU 3HDA
• 分子名称: Secreted protease C, Uncharacterized peptide, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: met-turn, beta roll, zinc, metalloprotease, metzincin, calcium, hydrolase, metal-binding, protease, secreted, zymogen
• 由来する生物種: Erwinia chrysanthemi; 詳細
• 細胞内の位置: Secreted: P16317
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50905.93

構造登録者

Oberholzer, A.E.,Bumann, M.,Hege, T.,Russo, S.,Baumann, U. (登録日: 2009-05-05, 公開日: 2009-06-30, 最終更新日: 2023-09-06)

主引用文献

Oberholzer, A.E.,Bumann, M.,Hege, T.,Russo, S.,Baumann, U.
Metzincin's canonical methionine is responsible for the structural integrity of the zinc-binding site
Biol.Chem., 390:875-881, 2009

PubMed Abstract: The metzincins constitute a subclan of metalloproteases possessing a HEXXHXXGXXH/D zinc-binding consensus sequence where the three histidines are zinc ligands and the glutamic acid is the catalytic base. A completely conserved methionine is located downstream of this motif. Families of the metzincin clan comprise, besides others, astacins, adamalysins proteases, matrix metallo-proteases, and serralysins. The latter are extracellular 50 kDa proteases secreted by Gram-negative bacteria via a type I secretion system. While there is a large body of structural and biochemical information available, the function of the conserved methionine has not been convincingly clarified yet. Here, we present the crystal structures of a number of mutants of the serralysin member protease C with the conserved methionine being replaced by Ile, Ala, and His. Together with our former report on the leucine and cysteine mutants, we demonstrate here that replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the chi(2) angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain.

PubMed: 19558324
DOI: 10.1515/BC.2009.100

実験手法

X-RAY DIFFRACTION (1.95 Å)