4tf4
From Proteopedia
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|PDB= 4tf4 |SIZE=350|CAPTION= <scene name='initialview01'>4tf4</scene>, resolution 2.0Å | |PDB= 4tf4 |SIZE=350|CAPTION= <scene name='initialview01'>4tf4</scene>, resolution 2.0Å | ||
|SITE= <scene name='pdbsite=AA1:Active+Site'>AA1</scene>, <scene name='pdbsite=AB1:Active+Site'>AB1</scene>, <scene name='pdbsite=CA1:Ca+Binding+Site'>CA1</scene>, <scene name='pdbsite=CA2:Ca+Binding+Site'>CA2</scene>, <scene name='pdbsite=CA3:Ca+Binding+Site'>CA3</scene> and <scene name='pdbsite=CA4:Ca+Binding+Site'>CA4</scene> | |SITE= <scene name='pdbsite=AA1:Active+Site'>AA1</scene>, <scene name='pdbsite=AB1:Active+Site'>AB1</scene>, <scene name='pdbsite=CA1:Ca+Binding+Site'>CA1</scene>, <scene name='pdbsite=CA2:Ca+Binding+Site'>CA2</scene>, <scene name='pdbsite=CA3:Ca+Binding+Site'>CA3</scene> and <scene name='pdbsite=CA4:Ca+Binding+Site'>CA4</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span> |
|GENE= BAMH1-PST1 FRAGMENT OF T. FUSC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2021 Thermobifida fusca]) | |GENE= BAMH1-PST1 FRAGMENT OF T. FUSC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2021 Thermobifida fusca]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tf4 OCA], [http://www.ebi.ac.uk/pdbsum/4tf4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=4tf4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Sakon, J.]] | [[Category: Sakon, J.]] | ||
[[Category: Wilson, D B.]] | [[Category: Wilson, D B.]] | ||
| - | [[Category: CA]] | ||
[[Category: alpha/alpha barrel]] | [[Category: alpha/alpha barrel]] | ||
[[Category: cellopentaose]] | [[Category: cellopentaose]] | ||
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[[Category: glycosyl hydrolase]] | [[Category: glycosyl hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:40:13 2008'' |
Revision as of 02:40, 31 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , and | ||||||
| Ligands: | , | ||||||
| Gene: | BAMH1-PST1 FRAGMENT OF T. FUSC (Thermobifida fusca) | ||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ENDO/EXOCELLULASE:CELLOPENTAOSE FROM THERMOMONOSPORA
Overview
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.
About this Structure
4TF4 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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