8J9C

Crystal structure of M61 peptidase (apo-form) from Xanthomonas campestris

8J9C の概要

• エントリーDOI: 10.2210/pdb8j9c/pdb
• 分子名称: Putative glycyl aminopeptidase, GLYCEROL, ZINC ION, ... (5 entities in total)
• 機能のキーワード: m61 peptidase, glycyl aminopeptidase, apo-form, hydrolase
• 由来する生物種: Xanthomonas campestris pv. campestris B100
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 291907.21

構造登録者

Yadav, P.,Kumar, A.,Jamdar, S.N.,Makde, R.D. (登録日: 2023-05-03, 公開日: 2024-05-01, 最終更新日: 2024-10-16)

主引用文献

Jamdar, S.N.,Yadav, P.,Kulkarni, B.S.,Kumar, A.,Makde, R.D.
Crystal structure of a newly identified M61 family aminopeptidase with broad substrate specificity that is solely responsible for recycling acidic amino acids.
Febs J., 291:3211-3232, 2024

PubMed Abstract: Aminopeptidases with varied substrate specificities are involved in different crucial physiological processes of cellular homeostasis. They also have wide applications in food and pharma industries. Within the bacterial cell, broad specificity aminopeptidases primarily participate in the recycling of amino acids by degrading oligopeptides generated via primary proteolysis mediated by cellular ATP-dependent proteases. However, in bacteria, a truly broad specificity enzyme, which can cleave off acidic, basic, Gly and hydrophobic amino acid residues, is extremely rare. Here, we report structure-function of a putative glycyl aminopeptidase (M61xc) from Xanthomonas campestris pv campestris (Xcc) belonging to the M61 peptidase family. The enzyme exhibits broad specificity and cleaves Ala, Leu, Asp, Glu, Met, Ser, Phe, Tyr, Gly, Arg, and Lys at the N terminus, optimally of peptides with a length of 3-7 amino acids. Further, we report the high-resolution crystal structure of M61xc in the apo form (2.1 Å) and bestatin-bound form (1.95 Å), detailing its catalytic and substrate preference mechanisms. Comparative analysis of enzyme activity in crude cell extracts from both wild-type and m61xc-knockout mutant strains of Xcc has elucidated the unique intracellular role of M61xc. This study suggests that M61xc is the exclusive enzyme in these bacteria that is responsible for liberating Asp/Glu residues from the N-termini of peptides. Also, in view of its broad specificity and peptide degradation ability, it could be considered equivalent to M1 or other oligomeric peptidases from families like M17, M18, M42 or S9, who have an important auxiliary role in post-proteasomal protein degradation in prokaryotes.

PubMed: 38646733
DOI: 10.1111/febs.17133

実験手法

X-RAY DIFFRACTION (2.1 Å)