Crystal Structure of a Periplasmic Substrate-Binding Protein in Complex with Calcium Lactate

被引:15
作者
Akiyama, Nobuhiko [1 ]
Takeda, Kazuki [1 ,2 ]
Miki, Kunio [1 ,2 ]
机构
[1] Kyoto Univ, Dept Chem, Grad Sch Sci, Sakyo Ku, Kyoto 6068502, Japan
[2] Harima Inst, RIKEN SPring Ctr 8, Sayo, Hyogo 6795148, Japan
关键词
periplasmic substrate-binding protein; calcium; lactate; TRAP transporter; crystal structure; EXTRACYTOPLASMIC-SOLUTE-RECEPTOR; METAL-LIGAND INTERACTIONS; TRAP TRANSPORTERS; LACTIC-ACID; FAMILY; PREDICTION; GEOMETRY;
D O I
10.1016/j.jmb.2009.07.043
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Lactate 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 11 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. (C) 2009 Elsevier Ltd. All rights reserved.
引用
收藏
页码:559 / 565
页数:7
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