1h1n

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{{STRUCTURE_1h1n| PDB=1h1n | SCENE= }}
{{STRUCTURE_1h1n| PDB=1h1n | SCENE= }}
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'''ATOMIC RESOLUTION STRUCTURE OF THE MAJOR ENDOGLUCANASE FROM THERMOASCUS AURANTIACUS'''
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===ATOMIC RESOLUTION STRUCTURE OF THE MAJOR ENDOGLUCANASE FROM THERMOASCUS AURANTIACUS===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12147244 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12147244}}
==About this Structure==
==About this Structure==
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[[Category: Thermophile]]
[[Category: Thermophile]]
[[Category: Thermophilic]]
[[Category: Thermophilic]]
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Revision as of 03:28, 1 July 2008

Image:1h1n.png

Template:STRUCTURE 1h1n

ATOMIC RESOLUTION STRUCTURE OF THE MAJOR ENDOGLUCANASE FROM THERMOASCUS AURANTIACUS

Template:ABSTRACT PUBMED 12147244

About this Structure

1H1N is a Single protein structure of sequence from Thermoascus aurantiacus. 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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