1g87: Difference between revisions

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<StructureSection load='1g87' size='340' side='right'caption='[[1g87]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='1g87' size='340' side='right'caption='[[1g87]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1g87]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/(in_press)_ruminiclostridium_cellulolyticum (in press) ruminiclostridium cellulolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G87 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1g87]] 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=1G87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G87 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.6&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CELCCG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1521 (in press) Ruminiclostridium cellulolyticum])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://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=1g87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g87 OCA], [https://pdbe.org/1g87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g87 RCSB], [https://www.ebi.ac.uk/pdbsum/1g87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g87 ProSAT]</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=1g87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g87 OCA], [https://pdbe.org/1g87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g87 RCSB], [https://www.ebi.ac.uk/pdbsum/1g87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g87 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cellulase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Aghajari, N]]
[[Category: Ruminiclostridium cellulolyticum]]
[[Category: Belaich, A]]
[[Category: Aghajari N]]
[[Category: Belaich, J P]]
[[Category: Belaich A]]
[[Category: Driguez, H]]
[[Category: Belaich JP]]
[[Category: Haser, R]]
[[Category: Driguez H]]
[[Category: Mandelman, D]]
[[Category: Haser R]]
[[Category: Beta barrel]]
[[Category: Mandelman D]]
[[Category: Cellulase 9g]]
[[Category: Cellulose binding domain]]
[[Category: Endoglucanase]]
[[Category: Hydrolase]]

Latest revision as of 06:09, 9 August 2023

THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM CELLULOLYTICUM

1g87, resolution 1.60Å

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