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| | <StructureSection load='1h0b' size='340' side='right'caption='[[1h0b]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='1h0b' size='340' side='right'caption='[[1h0b]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1h0b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43812 Atcc 43812]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H0B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1h0b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodothermus_marinus Rhodothermus marinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H0B FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</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]] 1.8Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></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=1h0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h0b OCA], [http://pdbe.org/1h0b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h0b RCSB], [http://www.ebi.ac.uk/pdbsum/1h0b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h0b 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=1h0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h0b OCA], [https://pdbe.org/1h0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h0b RCSB], [https://www.ebi.ac.uk/pdbsum/1h0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h0b ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O33897_RHOMR O33897_RHOMR] |
| | == 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: Atcc 43812]] | |
| - | [[Category: Cellulase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Crennell, S J]] | + | [[Category: Rhodothermus marinus]] |
| - | [[Category: Hreggvidsson, G O]] | + | [[Category: Crennell SJ]] |
| - | [[Category: Nordberg-Karlsson, E]] | + | [[Category: Hreggvidsson GO]] |
| - | [[Category: Endoglucanase]] | + | [[Category: Nordberg-Karlsson E]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
O33897_RHOMR
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Cellulose is one of the most abundant polysaccharides in nature and microorganisms have developed a comprehensive system for enzymatic breakdown of this ubiquitous carbon source, a subject of much interest in the biotechnology industry. Rhodothermus marinus produces a hyperthermostable cellulase, with a temperature optimum of more than 90 degrees C, the structure of which is presented here to 1.8 A resolution. The enzyme has been classified into glycoside hydrolase family 12; this is the first structure of a thermophilic member of this family to have been solved. The beta-jelly roll fold observed has identical topology to those of the two mesophilic members of the family whose structures have been elucidated previously. A Hepes buffer molecule bound in the active site may have triggered a conformational change to an active configuration as the two catalytic residues Glu124 and Glu207, together with dependent residues, are observed in a conformation similar to that seen in the structure of Streptomyces lividans CelB2 complexed with an inhibitor. The structural similarity between this cellulase and the mesophilic enzymes serves to highlight features that may be responsible for its thermostability, chiefly an increase in ion pair number and the considerable stabilisation of a mobile region seen in S. lividans CelB2. Additional aromatic residues in the active site region may also contribute to the difference in thermophilicity.
The structure of Rhodothermus marinus Cel12A, a highly thermostable family 12 endoglucanase, at 1.8 A resolution.,Crennell SJ, Hreggvidsson GO, Nordberg Karlsson E J Mol Biol. 2002 Jul 19;320(4):883-97. PMID:12095262[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Crennell SJ, Hreggvidsson GO, Nordberg Karlsson E. The structure of Rhodothermus marinus Cel12A, a highly thermostable family 12 endoglucanase, at 1.8 A resolution. J Mol Biol. 2002 Jul 19;320(4):883-97. PMID:12095262
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