1ly8: Difference between revisions

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{{Seed}}
[[Image:1ly8.png|left|200px]]


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==The crystal structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability and insight into modelling of protein structures==
The line below this paragraph, containing "STRUCTURE_1ly8", creates the "Structure Box" on the page.
<StructureSection load='1ly8' size='340' side='right'caption='[[1ly8]], [[Resolution|resolution]] 2.05&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'>[[1ly8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LY8 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]] 2.05&#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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
{{STRUCTURE_1ly8|  PDB=1ly8  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ly8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ly8 OCA], [https://pdbe.org/1ly8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ly8 RCSB], [https://www.ebi.ac.uk/pdbsum/1ly8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ly8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PER_COPCI PER_COPCI]
== 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/ly/1ly8_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=1ly8 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Seven amino-acid substitutions introduced into the 343 amino-acid-long sequence of Coprinus cinereus peroxidase (CiP) led to a mutant enzyme (TS-rCiP) which is more stable than the native enzyme at higher temperature, pH and hydrogen peroxide concentrations. It is therefore more suitable for industrial applications. A structure determination was conducted on a deglycosylated but still active form of TS-rCiP based on X-ray diffraction data to 2.05 A resolution measured on a crystal cooled to 100 K and refined to R = 0.202 and R(free) = 0.249. The increased stability of the TS-rCiP enzyme can be understood from the structural changes of the TS-rCiP structure revealed by a comparative analysis with other known CiP structures. One of the more significant changes caused by three of the substitutions, I49S, V53A and T121A, is the conversion of a hydrophobic pocket into a hydrophilic pocket with associated changes in the water structure and the hydrogen-bonding interactions. The E239G substitution, which gives rise to increased thermostability at high pH, creates changes in the water structure and in the orientation of a phenylalanine (Phe236) in its vicinity. The three substitutions M166F, M242 and Y242F introduced to increase the oxidative stability do not introduce any structural changes.


===The crystal structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability and insight into modelling of protein structures===
The structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability.,Houborg K, Harris P, Poulsen JC, Schneider P, Svendsen A, Larsen S Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):997-1003. Epub 2003, May 23. PMID:12777761<ref>PMID:12777761</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_12777761}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1ly8" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 12777761 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_12777761}}
__TOC__
 
</StructureSection>
==About this Structure==
1LY8 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LY8 OCA].
 
==Reference==
<ref group="xtra">PMID:12777761</ref><references group="xtra"/>
[[Category: Coprinopsis cinerea]]
[[Category: Coprinopsis cinerea]]
[[Category: Peroxidase]]
[[Category: Large Structures]]
[[Category: Harris, P.]]
[[Category: Harris P]]
[[Category: Houborg, K.]]
[[Category: Houborg K]]
[[Category: Larsen, S.]]
[[Category: Larsen S]]
[[Category: Poulsen, J C.N.]]
[[Category: Poulsen J-CN]]
[[Category: Schneider, P.]]
[[Category: Schneider P]]
[[Category: Svendsen, A.]]
[[Category: Svendsen A]]
[[Category: Coprinus cinereus]]
[[Category: Mutant]]
[[Category: Peroxidase]]
[[Category: Thermostability]]
 
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Retrieved from "https://proteopedia.org/1ly8"