5KD5

BT_4244 metallopeptidase from Bacteroides thetaiotaomicron

5KD5 の概要

• エントリーDOI: 10.2210/pdb5kd5/pdb
• 関連するPDBエントリー: 5KD2 5KD8 5KDJ 5KDN 5KDS 5KDU 5KDV 5KDW 5KDX
• 分子名称: Metallopeptidase, ZINC ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: o-glycopeptidase, pf13402/m60-like, hydrolase
• 由来する生物種: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 64618.70

構造登録者

Noach, I.,Boraston, A.B. (登録日: 2016-06-07, 公開日: 2017-01-11, 最終更新日: 2023-09-27)

主引用文献

Noach, I.,Ficko-Blean, E.,Pluvinage, B.,Stuart, C.,Jenkins, M.L.,Brochu, D.,Buenbrazo, N.,Wakarchuk, W.,Burke, J.E.,Gilbert, M.,Boraston, A.B.
Recognition of protein-linked glycans as a determinant of peptidase activity.
Proc. Natl. Acad. Sci. U.S.A., 114:E679-E688, 2017

PubMed Abstract: The vast majority of proteins are posttranslationally altered, with the addition of covalently linked sugars (glycosylation) being one of the most abundant modifications. However, despite the hydrolysis of protein peptide bonds by peptidases being a process essential to all life on Earth, the fundamental details of how peptidases accommodate posttranslational modifications, including glycosylation, has not been addressed. Through biochemical analyses and X-ray crystallographic structures we show that to hydrolyze their substrates, three structurally related metallopeptidases require the specific recognition of O-linked glycan modifications via carbohydrate-specific subsites immediately adjacent to their peptidase catalytic machinery. The three peptidases showed selectivity for different glycans, revealing protein-specific adaptations to particular glycan modifications, yet always cleaved the peptide bond immediately preceding the glycosylated residue. This insight builds upon the paradigm of how peptidases recognize substrates and provides a molecular understanding of glycoprotein degradation.

PubMed: 28096352
DOI: 10.1073/pnas.1615141114

実験手法

X-RAY DIFFRACTION (1.65 Å)