1h1n
From Proteopedia
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| - | [[Image:1h1n.jpg|left|200px]]<br /><applet load="1h1n" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1h1n, resolution 1.12Å" /> | ||
| - | '''ATOMIC RESOLUTION STRUCTURE OF THE MAJOR ENDOGLUCANASE FROM THERMOASCUS AURANTIACUS'''<br /> | ||
| - | == | + | ==Atomic resolution structure of the major endoglucanase from Thermoascus aurantiacus== |
| + | <StructureSection load='1h1n' size='340' side='right'caption='[[1h1n]], [[Resolution|resolution]] 1.12Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1h1n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoascus_aurantiacus Thermoascus aurantiacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H1N FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.12Å</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=1h1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h1n OCA], [https://pdbe.org/1h1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h1n RCSB], [https://www.ebi.ac.uk/pdbsum/1h1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h1n ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q8TG26_THEAU Q8TG26_THEAU] | ||
| + | == 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/h1/1h1n_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1h1n ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The crystal structure of the major endoglucanase from the thermophilic fungus Thermoascus aurantiacus was determined by single isomorphous replacement at 1.12A resolution. The full sequence supports the classification of the protein in a subgroup of glycoside hydrolase family 5 for which no structural data are available yet. The active site shows eight critical residues, strictly conserved within family 5. In addition, aromatic residues that line the substrate-binding cleft and that are possibly involved in substrate-binding are identified. A number of residues seem to be conserved among members of the subtype, including a disulphide bridge between Cys212 and Cys249. | The crystal structure of the major endoglucanase from the thermophilic fungus Thermoascus aurantiacus was determined by single isomorphous replacement at 1.12A resolution. The full sequence supports the classification of the protein in a subgroup of glycoside hydrolase family 5 for which no structural data are available yet. The active site shows eight critical residues, strictly conserved within family 5. In addition, aromatic residues that line the substrate-binding cleft and that are possibly involved in substrate-binding are identified. A number of residues seem to be conserved among members of the subtype, including a disulphide bridge between Cys212 and Cys249. | ||
| - | + | Atomic resolution structure of the major endoglucanase from Thermoascus aurantiacus.,Van Petegem F, Vandenberghe I, Bhat MK, Van Beeumen J Biochem Biophys Res Commun. 2002 Aug 9;296(1):161-6. PMID:12147244<ref>PMID:12147244</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1h1n" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Glucanase 3D structures|Glucanase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermoascus aurantiacus]] | ||
| + | [[Category: Bhat MK]] | ||
| + | [[Category: Van Beeumen J]] | ||
| + | [[Category: Van Petegem F]] | ||
| + | [[Category: Vandenberghe I]] | ||
Current revision
Atomic resolution structure of the major endoglucanase from Thermoascus aurantiacus
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