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3vhq

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[[Image:3vhq.jpg|left|200px]]
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==Crystal structure of the Ca6 site mutant of Pro-SA-subtilisin==
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<StructureSection load='3vhq' size='340' side='right' caption='[[3vhq]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3vhq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermococcus_kodakarensis Thermococcus kodakarensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VHQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VHQ FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2e1p|2e1p]], [[2zwo|2zwo]], [[2zwp|2zwp]]</td></tr>
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<tr><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=311400 Thermococcus kodakarensis])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vhq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vhq RCSB], [http://www.ebi.ac.uk/pdbsum/3vhq PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Tk-subtilisin, a hyperthermostable subtilisin-like serine protease from Thermococcus kodakarensis, matures from the inactive precursor, Pro-Tk-subtilisin (Pro-TKS), upon autoprocessing and degradation of the propeptide (Tkpro). It contains seven Ca(2+) ions. Four of them (Ca2-Ca5) are responsible for folding of Tk-subtilisin. In this study, to clarify the role of the other three Ca(2+) ions (Ca1, Ca6, and Ca7), we constructed Pro-TKS derivatives lacking the Ca1 ion (Pro-TKS/DeltaCa1), Ca6 ion (Pro-TKS/DeltaCa6), and Ca7 ion (Pro-TKS/DeltaCa7), and their active site mutants (Pro-S324A/DeltaCa1, Pro-S324A/DeltaCa6, and Pro-S324A/DeltaCa7, respectively). Pro-TKS/DeltaCa6 and Pro-TKS/DeltaCa7 fully matured into their active forms upon incubation at 80 degrees C for 30 min as did Pro-TKS. The mature enzymes were as active as Tk-subtilisin at 80 degrees C, indicating that the Ca6 and Ca7 ions are not important for activity. In contrast, Pro-TKS/DeltaCa1 matured poorly at 80 degrees C because of the instability of its mature domain. The enzymatic activity of Tk-subtilisin/DeltaCa1 was determined to be 50% of that of Tk-subtilisin using the refolded protein. This result suggests that the Ca1 ion is required for the maximal activity of Tk-subtilisin. The refolding rates of all Pro-S324A derivatives were comparable to that of Pro-S324A (active site mutant of Pro-TKS), indicating that these Ca(2+) ions are not needed for folding of Tk-subtilisin. The stabilities of Pro-S324A/DeltaCa1 and Pro-S324A/DeltaCa6 were decreased by 26.6 and 11.7 degrees C, respectively, in T(m) compared to that of Pro-S324A. The half-lives of Tk-subtilisin/DeltaCa6 and Tk-subtilisin/DeltaCa7 at 95 degrees C were 8- and 4-fold lower than that of Tk-subtilisin, respectively. These results suggest that the Ca1, Ca6, and Ca7 ions, especially the Ca1 ion, contribute to the hyperthermostabilization of Tk-subtilisin.
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{{STRUCTURE_3vhq| PDB=3vhq | SCENE= }}
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Requirement of Ca(2+) Ions for the Hyperthermostability of Tk-Subtilisin from Thermococcus kodakarensis.,Uehara R, Takeuchi Y, Tanaka SI, Takano K, Koga Y, Kanaya S Biochemistry. 2012 Jun 19. PMID:22686281<ref>PMID:22686281</ref>
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===Crystal structure of the Ca6 site mutant of Pro-SA-subtilisin===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_22686281}}
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==See Also==
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*[[Subtilisin|Subtilisin]]
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==About this Structure==
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== References ==
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[[3vhq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermococcus_kodakarensis Thermococcus kodakarensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VHQ OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:022686281</ref><references group="xtra"/>
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[[Category: Subtilisin]]
[[Category: Subtilisin]]
[[Category: Thermococcus kodakarensis]]
[[Category: Thermococcus kodakarensis]]

Revision as of 07:36, 5 June 2014

Crystal structure of the Ca6 site mutant of Pro-SA-subtilisin

3vhq, resolution 2.15Å

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