2kr7

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<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=2kr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kr7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kr7 RCSB], [http://www.ebi.ac.uk/pdbsum/2kr7 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=2kr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kr7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kr7 RCSB], [http://www.ebi.ac.uk/pdbsum/2kr7 PDBsum]</span></td></tr>
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== Function ==
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[[http://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==

Revision as of 17:10, 24 December 2014

solution structure of Helicobacter pylori SlyD

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