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.
5owj
From Proteopedia
(Difference between revisions)
m (Protected "5owj" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | The | + | ==The dynamic dimer structure of the chaperone Trigger Factor (conformer 2)== |
| - | + | <StructureSection load='5owj' size='340' side='right' caption='[[5owj]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5owj]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OWJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OWJ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5owi|5owi]]</td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=5owj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5owj OCA], [http://pdbe.org/5owj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5owj RCSB], [http://www.ebi.ac.uk/pdbsum/5owj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5owj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TIG_ECOLI TIG_ECOLI]] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to nascent polypeptide chains via ribosomal protein L23 (PubMed:12226666). Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity.<ref>PMID:8633085</ref> <ref>PMID:8521806</ref> <ref>PMID:14726952</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Peptidylprolyl isomerase]] | ||
| + | [[Category: Burmann, B M]] | ||
| + | [[Category: Hiller, S]] | ||
| + | [[Category: Mazur, A]] | ||
| + | [[Category: Morgado, L]] | ||
| + | [[Category: Sharpe, T]] | ||
| + | [[Category: Chaperone]] | ||
| + | [[Category: Dimer]] | ||
Revision as of 06:10, 29 November 2017
The dynamic dimer structure of the chaperone Trigger Factor (conformer 2)
| |||||||||||
