2V8K

Structure of a Family 2 Pectate Lyase in Complex with Trigalacturonic Acid

2V8K の概要

• エントリーDOI: 10.2210/pdb2v8k/pdb
• 関連するPDBエントリー: 2V8I 2V8J
• 分子名称: PECTATE LYASE, beta-D-galactopyranuronic acid-(1-4)-alpha-D-galactopyranuronic acid-(1-4)-alpha-D-galactopyranuronic acid (3 entities in total)
• 機能のキーワード: lyase, pectate lyase, beta-elimination, pectin degradation
• 由来する生物種: YERSINIA ENTEROCOLITICA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 61803.88

構造登録者

Abbott, D.W.,Boraston, A.B. (登録日: 2007-08-08, 公開日: 2007-09-18, 最終更新日: 2024-05-08)

主引用文献

Abbott, D.W.,Boraston, A.B.
A Family 2 Pectate Lyase Displays a Rare Fold and Transition Metal-Assisted Beta-Elimination.
J.Biol.Chem., 282:35328-, 2007

PubMed Abstract: The family 2 pectate lyase from Yersinia enterocolitica (YePL2A), solved to 1.5A, reveals it to be the first prokaryotic protein reported to display the rare (alpha/alpha)(7) barrel fold. In addition to its apo form, we have also determined the structure of a metal-bound form of YePL2A (to 2.0A) and a trigalacturonic acid-bound substrate complex (to 2.1A) Although its fold is rare, the catalytic center of YePL2A can be superimposed with structurally unrelated families, underlining the conserved catalytic amino acid architecture of the beta-elimination mechanism. In addition to its overall structure, YePL2A also has two other unique features: 1) it utilizes a metal atom other than calcium for catalysis, and 2) its Brønstead base is in an alternate conformation and directly interacts with the uronate group of the substrate.

PubMed: 17881361
DOI: 10.1074/JBC.M705511200

実験手法

X-RAY DIFFRACTION (2.1 Å)