2VPO

High resolution structure of the periplasmic binding protein TeaA from TeaABC TRAP transporter of Halomonas elongata in complex with hydroxyectoine

Summary for 2VPO

• Entry DOI: 10.2210/pdb2vpo/pdb
• Related: 2VPN
• Descriptor: PERIPLASMIC SUBSTRATE BINDING PROTEIN, (4S,5S)-5-HYDROXY-2-METHYL-1,4,5,6-TETRAHYDROPYRIMIDINE-4-CARBOXYLIC ACID, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: sbp, ectoine, hydroxyectoine, trap transporter, periplasmic binding protein, transport
• Biological source: HALOMONAS ELONGATA
• Total number of polymer chains: 2
• Total formula weight: 71791.37

Authors

Kuhlmann, S.I.,Terwisscha van Scheltinga, A.C.,Bienert, R.,Kunte, H.J.,Ziegler, C. (deposition date: 2008-03-03, release date: 2008-08-26, Last modification date: 2024-05-08)

Primary citation

Kuhlmann, S.I.,Terwisscha Van Scheltinga, A.C.,Bienert, R.,Kunte, H.J.,Ziegler, C.
1.55 A Structure of the Ectoine Binding Protein Teaa of the Osmoregulated Trap-Transporter Teaabc from Halomonas Elongata.
Biochemistry, 47:9475-, 2008

PubMed Abstract: TeaABC from the moderate halophilic bacterium Halomonas elongata belongs to the tripartite ATP-independent periplasmic transporters (TRAP-T), a family of secondary transporters functioning in conjunction with periplasmic substrate binding proteins. TeaABC facilitates the uptake of the compatible solutes ectoine and hydroxyectoine that are accumulated in the cytoplasm under hyperosmotic stress to protect the cell from dehydration. TeaABC is the only known TRAP-T activated by osmotic stress. Currently, our knowledge on the osmoregulated compatible solute transporter is limited to ABC transporters or conventional secondary transporters. Therefore, this study presents the first detailed analysis of the molecular mechanisms underlying substrate recognition of the substrate binding protein of an osmoregulated TRAP-T. In the present study we were able to demonstrate by isothermal titration calorimetry measurements that TeaA is a high-affinity ectoine binding protein ( K d = 0.19 microM) that also has a significant but somewhat lower affinity to hydroxyectoine ( K d = 3.8 microM). Furthermore, we present the structure of TeaA in complex with ectoine at a resolution of 1.55 A and hydroxyectoine at a resolution of 1.80 A. Analysis of the TeaA binding pocket and comparison of its structure to other compatible solute binding proteins from ABC transporters reveal common principles in compatible solute binding but also significant differences like the solvent-mediated specific binding of ectoine to TeaA.

PubMed: 18702523
DOI: 10.1021/BI8006719

Experimental method

X-RAY DIFFRACTION (1.8 Å)