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.
2kr7
From Proteopedia
(Difference between revisions)
| (7 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2kr7.png|left|200px]] | ||
| - | + | ==solution structure of Helicobacter pylori SlyD== | |
| - | + | <StructureSection load='2kr7' size='340' side='right'caption='[[2kr7]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2kr7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KR7 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |
| - | == | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kr7 OCA], [https://pdbe.org/2kr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kr7 RCSB], [https://www.ebi.ac.uk/pdbsum/2kr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kr7 ProSAT]</span></td></tr> |
| - | [[2kr7]] is a 1 chain structure with sequence from [ | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SLYD_HELPY SLYD_HELPY] Folding helper with both chaperone and peptidyl-prolyl cis-trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa-Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity). Also involved in hydrogenase metallocenter assembly, probably by participating in the nickel insertion step. This function in hydrogenase biosynthesis requires chaperone activity and the presence of the metal-binding domain, but not PPIase activity (By similarity). | ||
==See Also== | ==See Also== | ||
*[[FK506 binding protein|FK506 binding protein]] | *[[FK506 binding protein|FK506 binding protein]] | ||
| - | *[[ | + | *[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]] |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | + | ||
[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Cheng | + | [[Category: Cheng T]] |
| - | [[Category: Li | + | [[Category: Li H]] |
| - | [[Category: Sun | + | [[Category: Sun H]] |
| - | [[Category: Sze | + | [[Category: Sze K]] |
| - | [[Category: Xia | + | [[Category: Xia W]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
solution structure of Helicobacter pylori SlyD
| |||||||||||
Categories: Helicobacter pylori | Large Structures | Cheng T | Li H | Sun H | Sze K | Xia W
