2vi0: Difference between revisions

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{{Seed}}
[[Image:2vi0.png|left|200px]]


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==Lichenase CtLic26 in complex with a thio-oligosaccharide==
The line below this paragraph, containing "STRUCTURE_2vi0", creates the "Structure Box" on the page.
<StructureSection load='2vi0' size='340' side='right'caption='[[2vi0]], [[Resolution|resolution]] 1.51&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'>[[2vi0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VI0 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]] 1.51&#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=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MGL:O1-METHYL-GLUCOSE'>MGL</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</scene></td></tr>
{{STRUCTURE_2vi0|  PDB=2vi0  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vi0 OCA], [https://pdbe.org/2vi0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vi0 RCSB], [https://www.ebi.ac.uk/pdbsum/2vi0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vi0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GUNH_ACET2 GUNH_ACET2] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
== 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/vi/2vi0_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=2vi0 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The substrate binding regions of a beta-1,3:1,4 glucanase are revealed through structural analysis with a thio-oligosaccharide and kinetics of enzyme variants.


===LICHENASE CTLIC26 IN COMPLEX WITH A THIO-OLIGOSACCHARIDE===
Probing the beta-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants.,Money VA, Cartmell A, Guerreiro CI, Ducros VM, Fontes CM, Gilbert HJ, Davies GJ Org Biomol Chem. 2008 Mar 7;6(5):851-3. Epub 2008 Feb 4. PMID:18292875<ref>PMID:18292875</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2vi0" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_18292875}}, adds the Publication Abstract to the page
*[[Glucanase 3D structures|Glucanase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 18292875 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_18292875}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Acetivibrio thermocellus]]
2VI0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VI0 OCA].
[[Category: Large Structures]]
 
[[Category: Davies GJ]]
==Reference==
[[Category: Ducros VM]]
Probing the beta-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants., Money VA, Cartmell A, Guerreiro CI, Ducros VM, Fontes CM, Gilbert HJ, Davies GJ, Org Biomol Chem. 2008 Mar 7;6(5):851-3. Epub 2008 Feb 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18292875 18292875]
[[Category: Money VA]]
 
How family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides: structure and activity of a Clostridium thermocellum lichenase, CtLic26A., Taylor EJ, Goyal A, Guerreiro CI, Prates JA, Money VA, Ferry N, Morland C, Planas A, Macdonald JA, Stick RV, Gilbert HJ, Fontes CM, Davies GJ, J Biol Chem. 2005 Sep 23;280(38):32761-7. Epub 2005 Jun 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15987675 15987675]
 
Substrate distortion by a lichenase highlights the different conformational itineraries harnessed by related glycoside hydrolases., Money VA, Smith NL, Scaffidi A, Stick RV, Gilbert HJ, Davies GJ, Angew Chem Int Ed Engl. 2006 Aug 4;45(31):5136-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16823793 16823793]
[[Category: Cellulase]]
[[Category: Clostridium thermocellum]]
[[Category: Single protein]]
[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
[[Category: Carbohydrate metabolism]]
[[Category: Cellulose degradation]]
[[Category: Enzyme glycoside hydrolase lichenase beta glucanase gh26 g]]
[[Category: Glycosidase]]
[[Category: Hydrolase]]
[[Category: Polysaccharide degradation]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 18 20:36:15 2009''

Latest revision as of 15:20, 13 December 2023

Lichenase CtLic26 in complex with a thio-oligosaccharide

2vi0, resolution 1.51Å

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