3HGM

Universal Stress Protein TeaD from the TRAP transporter TeaABC of Halomonas elongata

3HGM の概要

• エントリーDOI: 10.2210/pdb3hgm/pdb
• 分子名称: Universal Stress Protein TeaD, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: universal stress protein, rossmann fold, signaling protein
• 由来する生物種: Halomonas elongata
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 65111.39

構造登録者

Schweikhard, E.S.,Kuhlmann, S.I.,Ziegler, C.M. (登録日: 2009-05-14, 公開日: 2010-03-02, 最終更新日: 2023-11-01)

主引用文献

Schweikhard, E.S.,Kuhlmann, S.I.,Kunte, H.J.,Grammann, K.,Ziegler, C.M.
Structure and function of the universal stress protein TeaD and its role in regulating the ectoine transporter TeaABC of Halomonas elongata DSM 2581(T)
Biochemistry, 49:2194-2204, 2010

PubMed Abstract: The halophilic bacterium Halomonas elongata takes up the compatible solute ectoine via the osmoregulated TRAP transporter TeaABC. A fourth orf (teaD) is located adjacent to the teaABC locus that encodes a putative universal stress protein (USP). By RT-PCR experiments we proved a cotranscription of teaD along with teaABC. Deletion of teaD resulted in an enhanced uptake for ectoine by the transporter TeaABC and hence a negative activity regulation of TeaABC by TeaD. A transcriptional regulation via DNA binding could be excluded. ATP binding to native TeaD was shown by HPLC, and the crystal structure of TeaD was solved in complex with ATP to a resolution of 1.9 A by molecular replacement. TeaD forms a dimer-dimer complex with one ATP molecule bound to each monomer, which has a Rossmann-like alpha/beta overall fold. Our results reveal an ATP-dependent oligomerization of TeaD, which might have a functional role in the regulatory mechanism of TeaD. USP-encoding orfs, which are located adjacent to genes encoding for TeaABC homologues, could be identified in several other organisms, and their physiological role in balancing the internal cellular ectoine pool is discussed.

PubMed: 20113006
DOI: 10.1021/bi9017522

実験手法

X-RAY DIFFRACTION (1.9 Å)