3RLB
Crystal structure at 2.0 A of the S-component for thiamin from an ECF-type ABC transporter
Summary for 3RLB
Entry DOI | 10.2210/pdb3rlb/pdb |
Descriptor | ThiT, nonyl beta-D-glucopyranoside, 3-(4-AMINO-2-METHYL-PYRIMIDIN-5-YLMETHYL)-5-(2-HYDROXY-ETHYL)-4-METHYL-THIAZOL-3-IUM, ... (4 entities in total) |
Functional Keywords | s-component, ecf transporter, abc transporter, substrate-binding domain, membrane, thiamine-binding protein |
Biological source | Lactococcus lactis subsp. cremoris |
Total number of polymer chains | 2 |
Total formula weight | 46364.01 |
Authors | Erkens, G.B.,Berntsson, R.P.-A.,Fulyani, F.,Majsnerowska, M.,Vujicic-Zagar, A.,ter Beek, J.,Poolman, B.,Slotboom, D.J. (deposition date: 2011-04-19, release date: 2011-06-29, Last modification date: 2024-02-28) |
Primary citation | Erkens, G.B.,Berntsson, R.P.,Fulyani, F.,Majsnerowska, M.,Ter Beek, J.,Poolman, B.,Slotboom, D.J. The structural basis of modularity in ECF-type ABC transporters. Nat.Struct.Mol.Biol., 18:755-760, 2011 Cited by PubMed Abstract: Energy coupling factor (ECF) transporters are used for the uptake of vitamins in Prokarya. They consist of an integral membrane protein that confers substrate specificity (the S-component) and an energizing module that is related to ATP-binding cassette (ABC) transporters. S-components for different substrates often do not share detectable sequence similarity but interact with the same energizing module. Here we present the crystal structure of the thiamine-specific S-component ThiT from Lactococcus lactis at 2.0 Å. Extensive protein-substrate interactions explain its high binding affinity for thiamine (K(d) ~10(-10) M). ThiT has a fold similar to that of the riboflavin-specific S-component RibU, with which it shares only 14% sequence identity. Two alanines in a conserved motif (AxxxA) located on the membrane-embedded surface of the S-components mediate the interaction with the energizing module. Based on these findings, we propose a general transport mechanism for ECF transporters. PubMed: 21706007DOI: 10.1038/nsmb.2073 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report