2VLB

Structure of unliganded arylmalonate decarboxylase

2VLB の概要

• エントリーDOI: 10.2210/pdb2vlb/pdb
• 分子名称: ARYLMALONATE DECARBOXYLASE, BETA-MERCAPTOETHANOL, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: protein dynamics, lyase, amdase, decarboxylase, decarboxylation
• 由来する生物種: BORDETELLA BRONCHISEPTICA
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 105420.54

構造登録者

Kuettner, E.B.,Keim, A.,Kircher, M.,Rosmus, S.,Strater, N. (登録日: 2008-01-11, 公開日: 2008-03-18, 最終更新日: 2025-04-09)

主引用文献

Kuettner, E.B.,Keim, A.,Kircher, M.,Rosmus, S.,Strater, N.
Active Site Mobility Revealed by the Crystal Structure of Arylmalonate Decarboxylase from Bordetella Bronchiseptica
J.Mol.Biol., 377:386-, 2008

PubMed Abstract: Arylmalonate decarboxylase (AMDase) from Bordetella bronchiseptica catalyzes the enantioselective decarboxylation of arylmethylmalonates without the need for an organic cofactor or metal ion. The decarboxylation reaction is of interest for the synthesis of fine chemicals. As basis for an analysis of the catalytic mechanism of AMDase and for a rational enzyme design, we determined the X-ray structure of the enzyme up to 1.9 A resolution. Like the distantly related aspartate or glutamate racemases, AMDase has an aspartate transcarbamoylase fold consisting of two alpha/beta domains related by a pseudo dyad. However, the domain orientation of AMDase differs by about 30 degrees from that of the glutamate racemases, and also significant differences in active-site structures are observed. In the crystals, four independent subunits showing different conformations of active-site loops are present. This finding is likely to reflect the active-site mobility necessary for catalytic activity.

PubMed: 18258259
DOI: 10.1016/J.JMB.2007.12.069

実験手法

X-RAY DIFFRACTION (1.92 Å)