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==solution structure of Helicobacter pylori SlyD== | ==solution structure of Helicobacter pylori SlyD== | ||
<StructureSection load='2kr7' size='340' side='right'caption='[[2kr7 | <StructureSection load='2kr7' size='340' side='right'caption='[[2kr7]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2kr7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | </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> | ||
<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> | |||
</table> | </table> | ||
== Function == | == 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== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Helicobacter pylori]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cheng T]] | |||
[[Category: Cheng | [[Category: Li H]] | ||
[[Category: Li | [[Category: Sun H]] | ||
[[Category: Sun | [[Category: Sze K]] | ||
[[Category: Sze | [[Category: Xia W]] | ||
[[Category: Xia | |||
Revision as of 11:05, 18 January 2023
solution structure of Helicobacter pylori SlyDsolution structure of Helicobacter pylori SlyD
Structural highlights
FunctionSLYD_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 |
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