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4dt4
From Proteopedia
(Difference between revisions)
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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=4dt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dt4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dt4 RCSB], [http://www.ebi.ac.uk/pdbsum/4dt4 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=4dt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dt4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dt4 RCSB], [http://www.ebi.ac.uk/pdbsum/4dt4 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FKBX_ECOLI FKBX_ECOLI]] PPIases accelerate the folding of proteins. Substrate specificity investigated with 'Suc-Ala-Xaa-Pro-Phe-4-nitroanilide' where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile > Lys = Ala > Trp > His >> Gln. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 06:27, 25 December 2014
Crystal structure of the PPIase-chaperone SlpA with the chaperone binding site occupied by the linker of the purification tag
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