5CIM

Structure of Mycobacterium thermoresistibile GlgE in complex with maltose (cocrystallisation with maltose-1-phosphate) at 3.32A resolution

5CIM の概要

• エントリーDOI: 10.2210/pdb5cim/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: glge, maltose, gh13, maltosyltransferase, transferase
• 由来する生物種: Mycobacterium thermoresistibile ATCC 19527
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 155578.70

構造登録者

Mendes, V.,Blaszczyk, M.,Maranha, A.,Empadinhas, N.,Blundell, T.L. (登録日: 2015-07-13, 公開日: 2015-12-09, 最終更新日: 2024-01-10)

主引用文献

Mendes, V.,Blaszczyk, M.,Maranha, A.,Empadinhas, N.,Blundell, T.L.
Structure of Mycobacterium thermoresistibile GlgE defines novel conformational states that contribute to the catalytic mechanism.
Sci Rep, 5:17144-17144, 2015

PubMed Abstract: GlgE, an enzyme of the pathway that converts trehalose to α-glucans, is essential for Mycobacterium tuberculosis. Inhibition of GlgE, which transfers maltose from a maltose-1-phosphate donor to α-glucan/maltooligosaccharide chain acceptor, leads to a toxic accumulation of maltose-1-phosphate that culminates in cellular death. Here we describe the first high-resolution mycobacterial GlgE structure from Mycobacterium thermoresistibile at 1.96 Å. We show that the structure resembles that of M. tuberculosis and Streptomyces coelicolor GlgEs, reported before, with each protomer in the homodimer comprising five domains. However, in M. thermoresistibile GlgE we observe several conformational states of the S domain and provide evidence that its high flexibility is important for enzyme activity. The structures here reported shed further light on the interactions between the N-terminal domains and the catalytic domains of opposing chains and how they contribute to the catalytic reaction. Importantly this work identifies a useful surrogate system to aid the development of GlgE inhibitors against opportunistic and pathogenic mycobacteria.

PubMed: 26616850
DOI: 10.1038/srep17144

実験手法

X-RAY DIFFRACTION (3.32 Å)