1thm

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[[Image:1thm.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF THERMITASE AT 1.4 ANGSTROMS RESOLUTION==
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|PDB= 1thm |SIZE=350|CAPTION= <scene name='initialview01'>1thm</scene>, resolution 1.37&Aring;
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<StructureSection load='1thm' size='340' side='right'caption='[[1thm]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1thm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1THM FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Thermitase Thermitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.66 3.4.21.66] </span>
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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]] 1.37&#8491;</td></tr>
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|GENE=
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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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=1thm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1thm OCA], [https://pdbe.org/1thm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1thm RCSB], [https://www.ebi.ac.uk/pdbsum/1thm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1thm ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1thm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1thm OCA], [http://www.ebi.ac.uk/pdbsum/1thm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1thm RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/THET_THEVU THET_THEVU]
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== Evolutionary Conservation ==
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'''CRYSTAL STRUCTURE OF THERMITASE AT 1.4 ANGSTROMS RESOLUTION'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/th/1thm_consurf.spt"</scriptWhenChecked>
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The crystal structure of thermitase, a subtilisin-type serine proteinase from Thermoactinomyces vulgaris, was determined by X-ray diffraction at 1.4 A resolution. The structure was solved by a combination of molecular and isomorphous replacement. The starting model was that of subtilisin BPN' from the Protein Data Bank, determined at 2.5 A resolution. The high-resolution refinement was based on data collected using synchrotron radiation with a Fuji image plate as detector. The model of thermitase refined to a conventional R factor of 14.9% and contains 1997 protein atoms, 182 water molecules and two Ca ions. The tertiary structure of thermitase is similar to that of the other subtilisins although there are some significant differences in detail. Comparison with subtilisin BPN' revealed two major structural differences. The N-terminal region in thermitase, which is absent in subtilisin BPN', forms a number of contacts with the tight Ca2+ binding site and indeed provides the very tight binding of the Ca ion. In thermitase the loop of residues 60 to 65 forms an additional (10) beta-strand of the central beta-sheet and the second Ca2+ binding site that has no equivalent in the subtilisin BPN' structure. The observed differences in the Ca2+ binding and the increased number of ionic and aromatic interactions in thermitase are likely sources of the enhanced stability of thermitase.
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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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==About this Structure==
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</jmolCheckbox>
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1THM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THM OCA].
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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=1thm ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Crystal structure of thermitase at 1.4 A resolution., Teplyakov AV, Kuranova IP, Harutyunyan EH, Vainshtein BK, Frommel C, Hohne WE, Wilson KS, J Mol Biol. 1990 Jul 5;214(1):261-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2196375 2196375]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Thermitase]]
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[[Category: Thermoactinomyces vulgaris]]
[[Category: Thermoactinomyces vulgaris]]
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[[Category: Harutyunyan, E H.]]
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[[Category: Harutyunyan EH]]
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[[Category: Kuranova, I P.]]
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[[Category: Kuranova IP]]
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[[Category: Teplyakov, A V.]]
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[[Category: Teplyakov AV]]
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[[Category: hydrolase(serine protease)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:56:08 2008''
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CRYSTAL STRUCTURE OF THERMITASE AT 1.4 ANGSTROMS RESOLUTION

PDB ID 1thm

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