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3HGM

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

Summary for 3HGM
Entry DOI10.2210/pdb3hgm/pdb
DescriptorUniversal Stress Protein TeaD, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsuniversal stress protein, rossmann fold, signaling protein
Biological sourceHalomonas elongata
Total number of polymer chains4
Total formula weight65111.39
Authors
Schweikhard, E.S.,Kuhlmann, S.I.,Ziegler, C.M. (deposition date: 2009-05-14, release date: 2010-03-02, Last modification date: 2023-11-01)
Primary citationSchweikhard, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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