2bog

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[[Image:2bog.gif|left|200px]]
 
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{{Structure
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==Catalytic domain of endo-1,4-glucanase Cel6A mutant Y73S from Thermobifida fusca in complex with methyl cellobiosyl-4-thio-beta- cellobioside==
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|PDB= 2bog |SIZE=350|CAPTION= <scene name='initialview01'>2bog</scene>, resolution 1.04&Aring;
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<StructureSection load='2bog' size='340' side='right'caption='[[2bog]], [[Resolution|resolution]] 1.04&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Bgc+Binding+Site+For+Chain+X'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MGL:O1-METHYL-GLUCOSE'>MGL</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</scene>
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<table><tr><td colspan='2'>[[2bog]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BOG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BOG FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </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]] 1.04&#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=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=MGL:O1-METHYL-GLUCOSE'>MGL</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</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=2bog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bog OCA], [https://pdbe.org/2bog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bog RCSB], [https://www.ebi.ac.uk/pdbsum/2bog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bog 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=2bog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bog OCA], [http://www.ebi.ac.uk/pdbsum/2bog PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bog RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/GUN2_THEFU GUN2_THEFU]
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== Evolutionary Conservation ==
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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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/2bog_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2bog ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Endoglucanase Cel6A from Thermobifida fusca hydrolyzes the beta-1,4 linkages in cellulose at accessible points along the polymer. The structure of the catalytic domain of Cel6A from T. fusca in complex with a nonhydrolysable substrate analogue that acts as an inhibitor, methylcellobiosyl-4-thio-beta-cellobioside (Glc(2)-S-Glc(2)), has been determined to 1.5 A resolution. The glycosyl unit in subsite -1 was sterically hindered by Tyr73 and forced into a distorted (2)S(o) conformation. In the enzyme where Tyr73 was mutated to a serine residue, the hindrance was removed and the glycosyl unit in subsite -1 had a relaxed (4)C(1) chair conformation. The relaxed conformation was seen in two complex structures of the mutated enzyme, with cellotetrose (Glc(4)) at 1.64 A and Glc(2)-S-Glc(2) at 1.04 A resolution.
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'''CATALYTIC DOMAIN OF ENDO-1,4-GLUCANASE CEL6A MUTANT Y73S FROM THERMOBIFIDA FUSCA IN COMPLEX WITH METHYL CELLOBIOSYL-4-THIO-BETA-CELLOBIOSIDE'''
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Crystal structure of Thermobifida fusca endoglucanase Cel6A in complex with substrate and inhibitor: the role of tyrosine Y73 in substrate ring distortion.,Larsson AM, Bergfors T, Dultz E, Irwin DC, Roos A, Driguez H, Wilson DB, Jones TA Biochemistry. 2005 Oct 4;44(39):12915-22. PMID:16185060<ref>PMID:16185060</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2bog" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Endoglucanase Cel6A from Thermobifida fusca hydrolyzes the beta-1,4 linkages in cellulose at accessible points along the polymer. The structure of the catalytic domain of Cel6A from T. fusca in complex with a nonhydrolysable substrate analogue that acts as an inhibitor, methylcellobiosyl-4-thio-beta-cellobioside (Glc(2)-S-Glc(2)), has been determined to 1.5 A resolution. The glycosyl unit in subsite -1 was sterically hindered by Tyr73 and forced into a distorted (2)S(o) conformation. In the enzyme where Tyr73 was mutated to a serine residue, the hindrance was removed and the glycosyl unit in subsite -1 had a relaxed (4)C(1) chair conformation. The relaxed conformation was seen in two complex structures of the mutated enzyme, with cellotetrose (Glc(4)) at 1.64 A and Glc(2)-S-Glc(2) at 1.04 A resolution.
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2BOG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BOG OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Crystal structure of Thermobifida fusca endoglucanase Cel6A in complex with substrate and inhibitor: the role of tyrosine Y73 in substrate ring distortion., Larsson AM, Bergfors T, Dultz E, Irwin DC, Roos A, Driguez H, Wilson DB, Jones TA, Biochemistry. 2005 Oct 4;44(39):12915-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16185060 16185060]
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[[Category: Cellulase]]
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[[Category: Single protein]]
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[[Category: Thermobifida fusca]]
[[Category: Thermobifida fusca]]
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[[Category: Bergfors, T.]]
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[[Category: Bergfors T]]
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[[Category: Driguez, H.]]
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[[Category: Driguez H]]
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[[Category: Dultz, E.]]
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[[Category: Dultz E]]
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[[Category: Irwin, D C.]]
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[[Category: Irwin DC]]
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[[Category: Jones, T A.]]
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[[Category: Jones TA]]
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[[Category: Larsson, A M.]]
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[[Category: Larsson AM]]
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[[Category: Roos, A.]]
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[[Category: Roos A]]
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[[Category: Wilson, D B.]]
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[[Category: Wilson DB]]
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[[Category: endoglucanase]]
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[[Category: glycoside hydrolase family 6]]
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[[Category: methyl cellobiosyl-4-thio-beta-cellobioside]]
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[[Category: thermobifida fusca]]
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[[Category: tim a/b fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:09:22 2008''
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Current revision

Catalytic domain of endo-1,4-glucanase Cel6A mutant Y73S from Thermobifida fusca in complex with methyl cellobiosyl-4-thio-beta- cellobioside

PDB ID 2bog

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