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1h1n
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(New page: 200px<br /><applet load="1h1n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h1n, resolution 1.12Å" /> '''ATOMIC RESOLUTION ST...)
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Revision as of 23:58, 24 November 2007
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ATOMIC RESOLUTION STRUCTURE OF THE MAJOR ENDOGLUCANASE FROM THERMOASCUS AURANTIACUS
Overview
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.
About this Structure
1H1N is a Single protein structure of sequence from Thermoascus aurantiacus. Active as Cellulase, with EC number 3.2.1.4 Full crystallographic information is available from OCA.
Reference
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
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