1tf4: Difference between revisions

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-[[Image:1tf4.gif|left|200px]]<br />
-<applet load="1tf4" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1tf4, resolution 1.9&Aring;" />
-'''ENDO/EXOCELLULASE FROM THERMOMONOSPORA'''<br />
-==Overview==
+==ENDO/EXOCELLULASE FROM THERMOMONOSPORA==
-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.
+<StructureSection load='1tf4' size='340' side='right'caption='[[1tf4]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1tf4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TF4 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tf4 OCA], [https://pdbe.org/1tf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tf4 RCSB], [https://www.ebi.ac.uk/pdbsum/1tf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tf4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GUN4_THEFU GUN4_THEFU]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tf/1tf4_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1tf4 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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==
+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>
-TF4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Structure known Active Sites: AA1, AB1, CA1, CA2, CA3 and CA4. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TF4 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9334746 9334746]
+</div>
-[[Category: Cellulase]]
+<div class="pdbe-citations 1tf4" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
+==See Also==
+*[[Glucanase 3D structures|Glucanase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Thermobifida fusca]]
-[[Category: Karplus, P.A.]]
+[[Category: Karplus PA]]
-[[Category: Sakon, J.]]
+[[Category: Sakon J]]
-[[Category: Wilson, D.B.]]
+[[Category: Wilson DB]]
-[[Category: CA]]
-[[Category: cellulose degradation]]
-[[Category: glycosyl hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 12:31:20 2007''