4O7O

Crystal structure of Mycobacterium tuberculosis maltose kinase MaK

4O7O の概要

• エントリーDOI: 10.2210/pdb4o7o/pdb
• 関連するPDBエントリー: 4O7P
• 分子名称: Maltokinase, SULFATE ION (3 entities in total)
• 機能のキーワード: maltose kinase, kinase, atp binding, maltose binding, transferase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 99959.77

構造登録者

Li, J.,Guan, X.T.,Rao, Z.H. (登録日: 2013-12-26, 公開日: 2014-10-22, 最終更新日: 2024-02-28)

主引用文献

Li, J.,Guan, X.,Shaw, N.,Chen, W.,Dong, Y.,Xu, X.,Li, X.,Rao, Z.
Homotypic dimerization of a maltose kinase for molecular scaffolding.
Sci Rep, 4:6418-6418, 2014

PubMed Abstract: Mycobacterium tuberculosis (Mtb) uses maltose-1-phosphate to synthesize α-glucans that make up the major component of its outer capsular layer. Maltose kinase (MaK) catalyzes phosphorylation of maltose. The molecular basis for this phosphorylation is currently not understood. Here, we describe the first crystal structure of MtbMaK refined to 2.4 Å resolution. The bi-modular architecture of MtbMaK reveals a remarkably unique N-lobe. An extended sheet protrudes into ligand binding pocket of an adjacent monomer and contributes residues critical for kinase activity. Structure of the complex of MtbMaK bound with maltose reveals that maltose binds in a shallow cavity of the C-lobe. Structural constraints permit phosphorylation of α-maltose only. Surprisingly, instead of a Gly-rich loop, MtbMaK employs 'EQS' loop to tether ATP. Notably, this loop is conserved across all MaK homologues. Structures of MtbMaK presented here unveil features that are markedly different from other kinases and support the scaffolding role proposed for this kinase.

PubMed: 25245657
DOI: 10.1038/srep06418

実験手法

X-RAY DIFFRACTION (2.4006 Å)