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==THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM CELLULOLYTICUM COMPLEXED WITH CELLOBIOSE==
==THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM CELLULOLYTICUM COMPLEXED WITH CELLOBIOSE==
<StructureSection load='1ga2' size='340' side='right' caption='[[1ga2]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1ga2' size='340' side='right'caption='[[1ga2]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ga2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35319 Atcc 35319]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GA2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GA2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ga2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ruminiclostridium_cellulolyticum Ruminiclostridium cellulolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GA2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CELCCG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1521 ATCC 35319])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</scene>, <scene name='pdbligand=PRD_900021:beta-cellotriose'>PRD_900021</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></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=1ga2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ga2 OCA], [https://pdbe.org/1ga2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ga2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ga2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ga2 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ga2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ga2 OCA], [http://pdbe.org/1ga2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ga2 RCSB], [http://www.ebi.ac.uk/pdbsum/1ga2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ga2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GUNG_CLOCE GUNG_CLOCE]] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.  
[https://www.uniprot.org/uniprot/GUNG_RUMCH GUNG_RUMCH] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</div>
</div>
<div class="pdbe-citations 1ga2" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1ga2" style="background-color:#fffaf0;"></div>
==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 35319]]
[[Category: Large Structures]]
[[Category: Cellulase]]
[[Category: Ruminiclostridium cellulolyticum]]
[[Category: Aghajari, N]]
[[Category: Aghajari N]]
[[Category: Belaich, A]]
[[Category: Belaich A]]
[[Category: Belaich, J P]]
[[Category: Belaich JP]]
[[Category: Driguez, H]]
[[Category: Driguez H]]
[[Category: Haser, R]]
[[Category: Haser R]]
[[Category: Mandelman, D]]
[[Category: Mandelman D]]
[[Category: Cellobiose complex]]
[[Category: Cellulase 9g]]
[[Category: Cellulose binding domain]]
[[Category: Endoglucanase]]
[[Category: Hydrolase]]
Retrieved from "https://proteopedia.org/1ga2"