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3tf4

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|PDB= 3tf4 |SIZE=350|CAPTION= <scene name='initialview01'>3tf4</scene>, resolution 2.2&Aring;
|PDB= 3tf4 |SIZE=350|CAPTION= <scene name='initialview01'>3tf4</scene>, resolution 2.2&Aring;
|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>
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|LIGAND= <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>
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|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]
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|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])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tf4 OCA], [http://www.ebi.ac.uk/pdbsum/3tf4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3tf4 RCSB]</span>
}}
}}
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[[Category: Sakon, J.]]
[[Category: Sakon, J.]]
[[Category: Wilson, D B.]]
[[Category: Wilson, D B.]]
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[[Category: CA]]
 
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[[Category: GLC]]
 
[[Category: glycosyl hydrolase]]
[[Category: glycosyl hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:07:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:36:15 2008''

Revision as of 02:36, 31 March 2008


PDB ID 3tf4

Drag the structure with the mouse to rotate
, resolution 2.2Å
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:CELLOTRIOSE 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

3TF4 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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