3tec

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[[Image:3tec.jpg|left|200px]]
 
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==CALCIUM BINDING TO THERMITASE. CRYSTALLOGRAPHIC STUDIES OF THERMITASE AT 0, 5 AND 100 MM CALCIUM==
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The line below this paragraph, containing "STRUCTURE_3tec", creates the "Structure Box" on the page.
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<StructureSection load='3tec' size='340' side='right'caption='[[3tec]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3tec]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Poecilobdella_manillensis Poecilobdella manillensis] and [https://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TEC FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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&#8491;</td></tr>
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<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>
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{{STRUCTURE_3tec| PDB=3tec | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tec OCA], [https://pdbe.org/3tec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tec RCSB], [https://www.ebi.ac.uk/pdbsum/3tec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tec ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/THET_THEVU THET_THEVU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/te/3tec_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3tec ConSurf].
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<div style="clear:both"></div>
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'''CALCIUM BINDING TO THERMITASE. CRYSTALLOGRAPHIC STUDIES OF THERMITASE AT 0, 5 AND 100 MM CALCIUM'''
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==See Also==
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*[[Eglin|Eglin]]
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__TOC__
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==Overview==
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</StructureSection>
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The three-dimensional crystal structure of thermitase complexed with eglin-c in the presence of 100 mM calcium has been determined and refined at 2.0-A resolution to a R-factor of 16.8%. This crystal structure is compared with previously determined structures of thermitase at 0 and 5 mM calcium concentration. In the presence of 100 mM calcium all three calcium binding sites in thermitase are fully occupied. At 100 mM CaCl2 the "weak" calcium binding is occupied by a calcium ion, which is chelated by three protein ligands and four water molecules in a pentagonal bipyramid geometry. Thermitase has, apparently, a monovalent and divalent cation binding position at 2.5-A distance from each other at this site. At low calcium concentrations the monovalent-ion position is occupied by a sodium or potassium ion. The "medium strength" binding site shows in the presence of 100 mM CaCl2 a square antiprism arrangement with eight ligands, of which seven are donated by the protein. At low calcium concentrations we observe a distorted pentagonal bipyramid coordination at this site. The largest difference between these two conformations is observed for ligand Asp-60, which has two conformations with 0.8-A difference in C alpha positions. The "strong" calcium binding site has a pentagonal bipyramid coordination and is fully occupied in all three structures. Structural changes on binding calcium to the weak and "medium strength" calcium binding sites of thermitase are limited to the direct surroundings of these sites. Thermitase resembles in this respect subtilisin BPN' and does not exhibit long-range shifts as have been reported for proteinase K.
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[[Category: Large Structures]]
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[[Category: Poecilobdella manillensis]]
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==About this Structure==
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3TEC is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Hirudinaria_manillensis Hirudinaria manillensis] and [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEC OCA].
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==Reference==
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Calcium binding to thermitase. Crystallographic studies of thermitase at 0, 5, and 100 mM calcium., Gros P, Kalk KH, Hol WG, J Biol Chem. 1991 Feb 15;266(5):2953-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1993669 1993669]
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[[Category: Hirudinaria manillensis]]
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[[Category: Protein complex]]
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[[Category: Thermitase]]
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[[Category: Thermoactinomyces vulgaris]]
[[Category: Thermoactinomyces vulgaris]]
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[[Category: Gros, P.]]
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[[Category: Gros P]]
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[[Category: Hol, W G.J.]]
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[[Category: Hol WGJ]]
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[[Category: Kalk, K H.]]
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[[Category: Kalk KH]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:13:42 2008''
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Current revision

CALCIUM BINDING TO THERMITASE. CRYSTALLOGRAPHIC STUDIES OF THERMITASE AT 0, 5 AND 100 MM CALCIUM

PDB ID 3tec

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