3cp7: Difference between revisions
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< | ==Crystal structure of a thermostable serine protease AL20 from extremophilic microoganism== | ||
<StructureSection load='3cp7' size='340' side='right'caption='[[3cp7]], [[Resolution|resolution]] 1.39Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3cp7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nesterenkonia_aethiopica Nesterenkonia aethiopica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CP7 FirstGlance]. <br> | |||
or | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.39Å</td></tr> | ||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=3cp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cp7 OCA], [https://pdbe.org/3cp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cp7 RCSB], [https://www.ebi.ac.uk/pdbsum/3cp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cp7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D0VWT7_9MICC D0VWT7_9MICC] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cp/3cp7_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=3cp7 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A novel calcium-independent serine protease from an alkaliphilic bacterium, Nesterenkonia sp. AL20, has been purified and crystallized at 296 K using sodium formate as the main precipitant. This enzyme is optimally active at pH 10, exhibits high stability towards autolytic digestion and its stability is not affected by the presence of EDTA or detergents. The triangular prism-shaped crystals diffracted X-rays to beyond 1.5 A at a synchrotron beamline, with space group R3 and unit-cell parameters a = b = 92.26, c = 137.88 A. A complete data set has been collected to 1.39 A resolution. The asymmetric unit is estimated and confirmed by self-rotation function calculation to contain two molecules, giving a crystal Volume per protein mass (V(M)) of 2.68 A(3) Da(-1) and a solvent content of 54%. | |||
Crystallization and preliminary X-ray analysis of an alkaline serine protease from Nesterenkonia sp.,Bakhtiar S, Vevodova J, Hatti-Kaul R, Su XD Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):529-31. Epub 2003, Feb 21. PMID:012595716<ref>PMID:012595716</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3cp7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
= | <references/> | ||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Nesterenkonia aethiopica]] | [[Category: Nesterenkonia aethiopica]] | ||
[[Category: Nan | [[Category: Nan J]] | ||
[[Category: Su | [[Category: Su X-D]] | ||
[[Category: Yang | [[Category: Yang N]] | ||
Latest revision as of 12:46, 6 November 2024
Crystal structure of a thermostable serine protease AL20 from extremophilic microoganismCrystal structure of a thermostable serine protease AL20 from extremophilic microoganism
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA novel calcium-independent serine protease from an alkaliphilic bacterium, Nesterenkonia sp. AL20, has been purified and crystallized at 296 K using sodium formate as the main precipitant. This enzyme is optimally active at pH 10, exhibits high stability towards autolytic digestion and its stability is not affected by the presence of EDTA or detergents. The triangular prism-shaped crystals diffracted X-rays to beyond 1.5 A at a synchrotron beamline, with space group R3 and unit-cell parameters a = b = 92.26, c = 137.88 A. A complete data set has been collected to 1.39 A resolution. The asymmetric unit is estimated and confirmed by self-rotation function calculation to contain two molecules, giving a crystal Volume per protein mass (V(M)) of 2.68 A(3) Da(-1) and a solvent content of 54%. Crystallization and preliminary X-ray analysis of an alkaline serine protease from Nesterenkonia sp.,Bakhtiar S, Vevodova J, Hatti-Kaul R, Su XD Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):529-31. Epub 2003, Feb 21. PMID:012595716[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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