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3tf4

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[[Image:3tf4.jpg|left|200px]]
 
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{{Structure
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==ENDO/EXOCELLULASE:CELLOTRIOSE FROM THERMOMONOSPORA==
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|PDB= 3tf4 |SIZE=350|CAPTION= <scene name='initialview01'>3tf4</scene>, resolution 2.2&Aring;
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<StructureSection load='3tf4' size='340' side='right' caption='[[3tf4]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|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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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>
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<table><tr><td colspan='2'>[[3tf4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TF4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TF4 FirstGlance]. <br>
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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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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|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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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAMH1-PST1 FRAGMENT OF T. FUSC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2021 "Thermonospora fusca" Henssen 1957])</td></tr>
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|DOMAIN=
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
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|RELATEDENTRY=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/3tf4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tf4 RCSB], [http://www.ebi.ac.uk/pdbsum/3tf4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tf4 ProSAT]</span></td></tr>
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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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</table>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tf/3tf4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3tf4 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''ENDO/EXOCELLULASE:CELLOTRIOSE FROM THERMOMONOSPORA'''
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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<ref>PMID:9334746</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3tf4" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Glucanase|Glucanase]]
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== References ==
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==About this Structure==
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<references/>
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3TF4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TF4 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Thermonospora fusca henssen 1957]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9334746 9334746]
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[[Category: Cellulase]]
[[Category: Cellulase]]
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[[Category: Single protein]]
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[[Category: Karplus, P A]]
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[[Category: Thermobifida fusca]]
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[[Category: Sakon, J]]
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[[Category: Karplus, P A.]]
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[[Category: Wilson, D B]]
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[[Category: Sakon, J.]]
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[[Category: Glycosyl hydrolase]]
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[[Category: Wilson, D B.]]
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[[Category: glycosyl hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:36:15 2008''
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Current revision

ENDO/EXOCELLULASE:CELLOTRIOSE FROM THERMOMONOSPORA

3tf4, resolution 2.20Å

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