1t2n: Difference between revisions

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{{Seed}}
[[Image:1t2n.png|left|200px]]


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==Structure of a thermostable triple mutant of Bacillus subtilis lipase obtained through directed evolution==
The line below this paragraph, containing "STRUCTURE_1t2n", creates the "Structure Box" on the page.
<StructureSection load='1t2n' size='340' side='right'caption='[[1t2n]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1t2n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T2N FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#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=K:POTASSIUM+ION'>K</scene></td></tr>
{{STRUCTURE_1t2n|  PDB=1t2n  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t2n OCA], [https://pdbe.org/1t2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t2n RCSB], [https://www.ebi.ac.uk/pdbsum/1t2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t2n ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ESTA_BACSU ESTA_BACSU] Active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups.<ref>PMID:8396026</ref>
== 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/t2/1t2n_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1t2n ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Variation in gene sequences generated by directed evolution approaches often does not assure a minimalist design for obtaining a desired property in proteins. While screening for enhanced thermostability, structural information was utilized in selecting mutations that are generated by error-prone PCR. By this approach we have increased the half-life of denaturation by 300-fold compared to the wild-type Bacillus subtilis lipase through three point mutations generated by only two cycles of error-prone PCR. At lower temperatures the activity parameters of the thermostable mutants are unaltered. High-resolution crystal structures of the mutants show subtle changes, which include stacking of tyrosine residues, peptide plane flipping and a better anchoring of the terminus, that challenge rational design and explain the structural basis for enhanced thermostability. The approach may offer an efficient and minimalist solution for the enhancement of a desired property of a protein.


===Structure of a thermostable triple mutant of Bacillus subtilis lipase obtained through directed evolution===
Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase.,Acharya P, Rajakumara E, Sankaranarayanan R, Rao NM J Mol Biol. 2004 Aug 27;341(5):1271-81. PMID:15321721<ref>PMID:15321721</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1t2n" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_15321721}}, adds the Publication Abstract to the page
*[[Lipase 3D Structures|Lipase 3D Structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 15321721 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_15321721}}
__TOC__
 
</StructureSection>
==About this Structure==
1T2N is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T2N OCA].
 
==Reference==
<ref group="xtra">PMID:15321721</ref><references group="xtra"/>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Triacylglycerol lipase]]
[[Category: Large Structures]]
[[Category: Rajakumara, E.]]
[[Category: Rajakumara E]]
[[Category: Sankaranarayanan, R.]]
[[Category: Sankaranarayanan R]]
[[Category: Alpha/beta hydrolase]]
 
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Retrieved from "https://proteopedia.org/1t2n"