6CAH

NMR-based structure of the FHA-2 domain from Mycobacterium tuberculosis ABC transporter Rv1747

6CAH の概要

• エントリーDOI: 10.2210/pdb6cah/pdb
• NMR情報: BMRB: 30399
• 分子名称: ABC transporter ATP-binding/permease protein Rv1747 (1 entity in total)
• 機能のキーワード: permuted forkhead-associated domain, beta-sandwich, phosphothreonine binding, abc transporter, protein binding
• 由来する生物種: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11602.13

構造登録者

Heinkel, F.,Okon, M.,Gsponer, J.,McIntosh, L.P. (登録日: 2018-01-30, 公開日: 2018-06-20, 最終更新日: 2024-05-15)

主引用文献

Heinkel, F.,Shen, L.,Richard-Greenblatt, M.,Okon, M.,Bui, J.M.,Gee, C.L.,Gay, L.M.,Alber, T.,Av-Gay, Y.,Gsponer, J.,McIntosh, L.P.
Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacterium tuberculosis ABC Transporter Rv1747.
Structure, 26:972-, 2018

PubMed Abstract: The Mycobacterium tuberculosis ATP-binding cassette transporter Rv1747 is a putative exporter of cell wall biosynthesis intermediates. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting Forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). The structures of FHA-1 and FHA-2 were determined by X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, respectively. Relative to the canonical 11-strand β-sandwich FHA domain fold of FHA-1, FHA-2 is circularly permuted and lacking one β-strand. Nevertheless, the two share a conserved pThr-binding cleft. FHA-2 is less stable and more dynamic than FHA-1, yet binds model pThr peptides with moderately higher affinity (∼50 μM versus 500 μM equilibrium dissociation constants). Based on NMR relaxation and chemical shift perturbation measurements, when joined within a polypeptide chain, either FHA domain can bind either linker pThr to form intra- and intermolecular complexes. We hypothesize that this enables tunable phosphorylation-dependent multimerization to regulate Rv1747 transporter activity.

PubMed: 29861345
DOI: 10.1016/j.str.2018.04.018

実験手法

SOLUTION NMR