Structural highlights
FunctionTLBP_THET8 Part of the tripartite ATP-independent periplasmic (TRAP) transport system involved in the uptake of lactate. This protein specifically binds L-lactate.[UniProtKB:P37676][1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedLactate is utilized in many biological processes, and its transport across biological membranes is mediated with various types of transporters. Here, we report the crystal structures of a lactate-binding protein of a TRAP (tripartite ATP-independent periplasmic) secondary transporter from Thermus thermophilus HB8. The folding of the protein is typical for a type II periplasmic solute-binding protein and forms a dimer in a back-to-back manner. One molecule of l-lactate is clearly identified in a cleft of the protein as a complex with a calcium ion. Detailed crystallographic and biochemical analyses revealed that the calcium ion can be removed from the protein and replaced with other divalent cations. This characterization of the structure of a protein binding with calcium lactate makes a significant contribution to our understanding of the mechanisms by which calcium and lactate are accommodated in cells. Crystal structure of a periplasmic substrate-binding protein in complex with calcium lactate.,Akiyama N, Takeda K, Miki K J Mol Biol. 2009 Sep 25;392(3):559-65. Epub 2009 Jul 22. PMID:19631222[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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