3vhq: Difference between revisions

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-[[Image:3vhq.jpg|left|200px]]
-{{STRUCTURE_3vhq|  PDB=3vhq  |  SCENE=  }}
+==Crystal structure of the Ca6 site mutant of Pro-SA-subtilisin==
+<StructureSection load='3vhq' size='340' side='right'caption='[[3vhq]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3vhq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3VHQ FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=3vhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vhq OCA], [https://pdbe.org/3vhq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vhq RCSB], [https://www.ebi.ac.uk/pdbsum/3vhq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vhq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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, 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.
-===Crystal structure of the Ca6 site mutant of Pro-SA-subtilisin===
+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>
-{{ABSTRACT_PUBMED_22686281}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3vhq" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-[[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].
+*[[Subtilisin 3D structures|Subtilisin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:022686281</ref><references group="xtra"/>
+__TOC__
-[[Category: Subtilisin]]
+</StructureSection>
-[[Category: Thermococcus kodakarensis]]
+[[Category: Large Structures]]
-[[Category: Kanaya, S.]]
+[[Category: Thermococcus kodakarensis KOD1]]
-[[Category: Koga, Y.]]
+[[Category: Kanaya S]]
-[[Category: Matsumura, H.]]
+[[Category: Koga Y]]
-[[Category: Takano, K.]]
+[[Category: Matsumura H]]
-[[Category: Takeuchi, Y.]]
+[[Category: Takano K]]
-[[Category: Tanaka, S.]]
+[[Category: Takeuchi Y]]
-[[Category: Uehara, R.]]
+[[Category: Tanaka S]]
-[[Category: Hydrolase]]
+[[Category: Uehara R]]
-[[Category: Proteolysis]]