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4jp8
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of Pro-F17H/S324A== | |
| - | === | + | <StructureSection load='4jp8' size='340' side='right' caption='[[4jp8]], [[Resolution|resolution]] 2.21Å' scene=''> |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4jp8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_kodakaraensis_(strain_kod1) Pyrococcus kodakaraensis (strain kod1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JP8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JP8 FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TK1675 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)])</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=4jp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jp8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jp8 RCSB], [http://www.ebi.ac.uk/pdbsum/4jp8 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/TKSU_THEKO TKSU_THEKO]] Has a broad substrate specificity with a slight preference to large hydrophobic amino acid residues at the P1 position. | [[http://www.uniprot.org/uniprot/TKSU_THEKO TKSU_THEKO]] Has a broad substrate specificity with a slight preference to large hydrophobic amino acid residues at the P1 position. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tk-subtilisin (Gly70-Gly398) is a subtilisin homolog from Thermococcus kodakarensis. Active Tk-subtilisin is produced from its inactive precursor, Pro-Tk-subtilisin (Gly1-Gly398), by autoprocessing and degradation of the propeptide (Tk-propeptide, Gly1-Leu69). This activation process is extremely slow at moderate temperatures owing to high stability of Tk-propeptide. Tk-propeptide is stabilized by the hydrophobic core. To examine whether a single nonpolar-to-polar amino acid substitution at this core affects the activation rate of Pro-Tk-subtilisin, the Pro-Tk-subtilisin derivative with the Phe17 --> His mutation (Pro-F17H), Tk-propeptide derivative with the same mutation (F17H-propeptide), and two active-site mutants of Pro-F17H (Pro-F17H/S324A and Pro-F17H/S324C) were constructed. The crystal structure of Pro-F17H/S324A was nearly identical to that of Pro-S324A, indicating that the mutation does not affect the structure of Pro-Tk-subtilisin. The refolding rate of Pro-F17H/S324A and autoprocessing rate of Pro-F17H/S324C were also nearly identical to those of their parent proteins (Pro-S324A and Pro-S324C). However, the activation rate of Pro-F17H greatly increased when compared with that of Pro-Tk-subtilisin, such that Pro-F17H is efficiently activated even at 40 degrees C. The far-UV circular dichroism spectrum of F17H-propeptide did not exhibit a broad trough at 205-230 nm, which is observed in the spectrum of Tk-propeptide. F17H-propeptide is more susceptible to chymotryptic degradation than Tk-propeptide. These results suggest that F17H-propeptide is unfolded in an isolated form and is therefore rapidly degraded by Tk-subtilisin. Thus, destabilization of the hydrophobic core of Tk-propeptide by a nonpolar-to-polar amino acid substitution is an effective way to increase the activation rate of Pro-Tk-subtilisin. | ||
| + | |||
| + | Increase in activation rate of Pro-Tk-subtilisin by a single nonpolar-to-polar amino acid substitution at the hydrophobic core of the propeptide domain.,Yuzaki K, Sanda Y, You DJ, Uehara R, Koga Y, Kanaya S Protein Sci. 2013 Dec;22(12):1711-21. doi: 10.1002/pro.2371. Epub 2013 Oct 19. PMID:24115021<ref>PMID:24115021</ref> | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | + | *[[Subtilisin|Subtilisin]] | |
| - | [[Category: Kanaya, S | + | == References == |
| - | [[Category: Koga, Y | + | <references/> |
| - | [[Category: Uehara, R | + | __TOC__ |
| - | [[Category: You, D J | + | </StructureSection> |
| - | [[Category: Yuzaki, K | + | [[Category: Kanaya, S]] |
| + | [[Category: Koga, Y]] | ||
| + | [[Category: Uehara, R]] | ||
| + | [[Category: You, D J]] | ||
| + | [[Category: Yuzaki, K]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Subtilisin-like serine protease]] | [[Category: Subtilisin-like serine protease]] | ||
[[Category: Subtillisin]] | [[Category: Subtillisin]] | ||
[[Category: Thermococcus kodakarensis]] | [[Category: Thermococcus kodakarensis]] | ||
Revision as of 14:46, 24 December 2014
Crystal structure of Pro-F17H/S324A
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