1js4

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{{STRUCTURE_1js4| PDB=1js4 | SCENE= }}
{{STRUCTURE_1js4| PDB=1js4 | SCENE= }}
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'''ENDO/EXOCELLULASE:CELLOBIOSE FROM THERMOMONOSPORA'''
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===ENDO/EXOCELLULASE:CELLOBIOSE FROM THERMOMONOSPORA===
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==Overview==
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Cellulase E4 from Thermomonospora fusca is unusual in that it has characteristics of both exo- and endo-cellulases. Here we report the crystal structure of a 68K M(r) fragment of E4 (E4-68) at 1.9 A resolution. E4-68 contains both a family 9 catalytic domain, exhibiting an (alpha/alpha)6 barrel fold, and a family III cellulose binding domain, having an antiparallel beta-sandwich fold. While neither of these folds is novel, E4-68 provides the first cellulase structure having interacting catalytic and cellulose binding domains. The complexes of E4-68 with cellopentaose, cellotriose and cellobiose reveal conformational changes associated with ligand binding and allow us to propose a catalytic mechanism for family 9 enzymes. We also provide evidence that E4 has two novel characteristics: first it combines exo- and endo-activities and second, when it functions as an exo-cellulase, it cleaves off cellotetraose units.
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(as it appears on PubMed at http://www.pubmed.gov), where 9334746 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9334746}}
==About this Structure==
==About this Structure==
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[[Category: Wilson, D B.]]
[[Category: Wilson, D B.]]
[[Category: Glycosyl hydrolase]]
[[Category: Glycosyl hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:48:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:43:19 2008''

Revision as of 17:43, 1 July 2008

Image:1js4.png

Template:STRUCTURE 1js4

ENDO/EXOCELLULASE:CELLOBIOSE FROM THERMOMONOSPORA

Template:ABSTRACT PUBMED 9334746

About this Structure

1JS4 is a Single protein structure of sequence from Thermobifida fusca. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca., Sakon J, Irwin D, Wilson DB, Karplus PA, Nat Struct Biol. 1997 Oct;4(10):810-8. PMID:9334746

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