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| - | [[Image:1tml.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1tml| PDB=1tml | SCENE= }} | | {{STRUCTURE_1tml| PDB=1tml | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A THERMOPHILIC ENDOCELLULASE'''
| + | ===CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A THERMOPHILIC ENDOCELLULASE=== |
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| - | ==Overview==
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| - | One way to improve the economic feasibility of biomass conversion is to enhance the catalytic efficiency of cellulases through protein engineering. This requires that high-resolution structures of cellulases be available. Here we present the structure of E2cd, the catalytic domain of the thermophilic endocellulase E2 from Thermomonospora fusca, as determined by X-ray crystallography. The structure was solved by multiple isomorphous replacement at 2.6-A resolution and has been refined at 1.8-A resolution to an R-value of 18.4% for all reflections between 10- and 1.8-A resolution. The fold of E2cd is based on an unusual parallel beta-barrel and is equivalent to the fold determined for the catalytic domain of cellobiohydrolase II, an exocellulase from Trichoderma reesei [Rouvinen et al. (1990) Science 249, 380-385]. The active site cleft of the enzyme, approximately 11 A deep and running the entire length of the molecule, is seen to be completely free for ligand binding in the crystal. A 2.2-A resolution analysis of crystals of E2cd complexed with cellobiose, an inhibitor, shows how cellobiose binds in the active site and interacts with several residues which line the cleft. Catalytic roles are suggested for three aspartic acid residues at the active site. A comparison of the E2cd and CBHIIcd structures reveals a large difference in their active site accessibilities and supports the hypothesis that the main difference between endo- and exocellulases is the degree to which their active sites are accessible to substrate.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8399160}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8399160 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8399160}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Beta-amylase]] | | [[Category: Beta-amylase]] |
| | [[Category: Endocellulase,catalytic domain]] | | [[Category: Endocellulase,catalytic domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:07:59 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:26:59 2008'' |
Revision as of 11:27, 27 July 2008
Template:STRUCTURE 1tml
CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A THERMOPHILIC ENDOCELLULASE
Template:ABSTRACT PUBMED 8399160
About this Structure
1TML is a Single protein structure of sequence from Thermobifida fusca. Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic domain of a thermophilic endocellulase., Spezio M, Wilson DB, Karplus PA, Biochemistry. 1993 Sep 28;32(38):9906-16. PMID:8399160
Page seeded by OCA on Sun Jul 27 14:26:59 2008
