This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4z7f
From Proteopedia
(Difference between revisions)
| Line 6: | Line 6: | ||
<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=4z7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z7f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4z7f RCSB], [http://www.ebi.ac.uk/pdbsum/4z7f PDBsum]</span></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=4z7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z7f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4z7f RCSB], [http://www.ebi.ac.uk/pdbsum/4z7f PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Energy-coupling factor (ECF) transporters are a new family of ABC transporters that consist of four subunits, two cytoplasmic ATPases EcfA and EcfA' and two transmembrane proteins namely EcfS for substrate-specific binding and EcfT for energy coupling. Here, we report the 3.2-A resolution crystal structure of the EcfS protein of a folate ECF transporter from Enterococcus faecalis-EfFolT, a close homologue of FolT from Lactobacillus brevis-LbFolT. Structural and biochemical analyses reveal the residues constituting the folate-binding pocket and determining the substrate-binding specificity. Structural comparison of the folate-bound EfFolT with the folate-free LbFolT contained in the holotransporter complex discloses significant conformational change at the L1 loop, and reveals a gating mechanism of ECF transporters in which the L1 loop of EcfS acts as a gate in the substrate binding and release. | ||
| + | |||
| + | Structures of FolT in substrate-bound and substrate-released conformations reveal a gating mechanism for ECF transporters.,Zhao Q, Wang C, Wang C, Guo H, Bao Z, Zhang M, Zhang P Nat Commun. 2015 Jul 22;6:7661. doi: 10.1038/ncomms8661. PMID:26198469<ref>PMID:26198469</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:43, 5 August 2015
Crystal structure of FolT bound with folic acid
| |||||||||||
