6fnp: Difference between revisions
m Protected "6fnp" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of ECF-CbrT, a cobalamin transporter== | |||
<StructureSection load='6fnp' size='340' side='right' caption='[[6fnp]], [[Resolution|resolution]] 3.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fnp]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FNP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FNP FirstGlance]. <br> | |||
</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=6fnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fnp OCA], [http://pdbe.org/6fnp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fnp RCSB], [http://www.ebi.ac.uk/pdbsum/6fnp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fnp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/A0A061BSU4_LACDE A0A061BSU4_LACDE]] Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.[HAMAP-Rule:MF_01461] [[http://www.uniprot.org/uniprot/ECFA2_LACDA ECFA2_LACDA]] ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. [[http://www.uniprot.org/uniprot/ECFA1_LACDA ECFA1_LACDA]] ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Vitamin B12 (cobalamin) is the most complex B-type vitamin and is synthetized exclusively in a limited number of prokaryotes. Its biologically active variants contain rare organometallic bonds, which are used by enzymes in a variety of central metabolic pathways such as L-methionine synthesis and ribonucleotide reduction. Although its biosynthesis and role as co-factor are well understood, knowledge about uptake of cobalamin by prokaryotic auxotrophs is scarce. Here, we characterize a cobalamin-specific ECF-type ABC transporter from Lactobacillus delbrueckii, ECF-CbrT, and demonstrate that it mediates the specific, ATP-dependent uptake of cobalamin. We solved the crystal structure of ECF-CbrT in an apo conformation to 3.4 A resolution. Comparison with the ECF transporter for folate (ECF-FolT2) from the same organism, reveals how the identical ECF module adjusts to interact with the different substrate binding proteins FolT2 and CbrT. ECF-CbrT is unrelated to the well-characterized B12 transporter BtuCDF, but their biochemical features indicate functional convergence. | |||
Functional and structural characterization of an ECF-type ABC transporter for vitamin B12.,Santos JA, Rempel S, Mous ST, Pereira CT, Ter Beek J, de Gier JW, Guskov A, Slotboom DJ Elife. 2018 May 29;7. pii: 35828. doi: 10.7554/eLife.35828. PMID:29809140<ref>PMID:29809140</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6fnp" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Guskov, A]] | |||
[[Category: Rempel, S]] | |||
[[Category: Santos, J A]] | |||
[[Category: Slotboom, D J]] | |||
[[Category: Abc transporter]] | |||
[[Category: Cobalamin]] | |||
[[Category: Ecf transporter]] | |||
[[Category: Membrane protein]] | |||
[[Category: Transport protein]] | |||
[[Category: Vitamin b12]] | |||
Latest revision as of 10:22, 25 July 2018
Crystal structure of ECF-CbrT, a cobalamin transporterCrystal structure of ECF-CbrT, a cobalamin transporter
Structural highlights
Function[A0A061BSU4_LACDE] Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.[HAMAP-Rule:MF_01461] [ECFA2_LACDA] ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. [ECFA1_LACDA] ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. Publication Abstract from PubMedVitamin B12 (cobalamin) is the most complex B-type vitamin and is synthetized exclusively in a limited number of prokaryotes. Its biologically active variants contain rare organometallic bonds, which are used by enzymes in a variety of central metabolic pathways such as L-methionine synthesis and ribonucleotide reduction. Although its biosynthesis and role as co-factor are well understood, knowledge about uptake of cobalamin by prokaryotic auxotrophs is scarce. Here, we characterize a cobalamin-specific ECF-type ABC transporter from Lactobacillus delbrueckii, ECF-CbrT, and demonstrate that it mediates the specific, ATP-dependent uptake of cobalamin. We solved the crystal structure of ECF-CbrT in an apo conformation to 3.4 A resolution. Comparison with the ECF transporter for folate (ECF-FolT2) from the same organism, reveals how the identical ECF module adjusts to interact with the different substrate binding proteins FolT2 and CbrT. ECF-CbrT is unrelated to the well-characterized B12 transporter BtuCDF, but their biochemical features indicate functional convergence. Functional and structural characterization of an ECF-type ABC transporter for vitamin B12.,Santos JA, Rempel S, Mous ST, Pereira CT, Ter Beek J, de Gier JW, Guskov A, Slotboom DJ Elife. 2018 May 29;7. pii: 35828. doi: 10.7554/eLife.35828. PMID:29809140[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||