3rlb

<StructureSection load='3rlb' size='340' side='right' caption='[[3rlb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[3rlb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lacln Lacln]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RLB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RLB FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=VIB:3-(4-AMINO-2-METHYL-PYRIMIDIN-5-YLMETHYL)-5-(2-HYDROXY-ETHYL)-4-METHYL-THIAZOL-3-IUM'>VIB</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LLNZ_01755 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=746361 LACLN])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rlb OCA], [http://pdbe.org/3rlb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rlb RCSB], [http://www.ebi.ac.uk/pdbsum/3rlb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rlb ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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 A. 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.

The structural basis of modularity in ECF-type ABC transporters.,Erkens GB, Berntsson RP, Fulyani F, Majsnerowska M, Vujicic-Zagar A, Ter Beek J, Poolman B, Slotboom DJ Nat Struct Mol Biol. 2011 Jun 26;18(7):755-60. doi: 10.1038/nsmb.2073. PMID:21706007<ref>PMID:21706007</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3rlb" style="background-color:#fffaf0;"></div>

*[[ABC transporter|ABC transporter]]

[[Category: Lacln]]

[[Category: Beek, J ter]]

[[Category: Berntsson, R P.A]]

[[Category: Erkens, G B]]

[[Category: Fulyani, F]]

[[Category: Majsnerowska, M]]

[[Category: Poolman, B]]

[[Category: Slotboom, D J]]

[[Category: Vujicic-Zagar, A]]

[[Category: Abc transporter]]

[[Category: Thiamine-binding protein]]