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1tml

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[[Image:1tml.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A THERMOPHILIC ENDOCELLULASE==
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|PDB= 1tml |SIZE=350|CAPTION= <scene name='initialview01'>1tml</scene>, resolution 1.8&Aring;
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<StructureSection load='1tml' size='340' side='right'caption='[[1tml]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1tml]] is a 1 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=1TML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TML 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tml OCA], [https://pdbe.org/1tml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tml RCSB], [https://www.ebi.ac.uk/pdbsum/1tml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tml ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tml OCA], [http://www.ebi.ac.uk/pdbsum/1tml PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tml RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/GUN2_THEFU GUN2_THEFU]
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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/tm/1tml_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=1tml ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A THERMOPHILIC ENDOCELLULASE'''
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==See Also==
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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==About this Structure==
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1TML 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=1TML OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8399160 8399160]
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[[Category: Cellulase]]
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[[Category: Single protein]]
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[[Category: Thermobifida fusca]]
[[Category: Thermobifida fusca]]
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[[Category: Karplus, P A.]]
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[[Category: Karplus PA]]
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[[Category: Spezio, M.]]
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[[Category: Spezio M]]
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[[Category: Wilson, D B.]]
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[[Category: Wilson DB]]
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[[Category: beta-amylase]]
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[[Category: endocellulase,catalytic domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:58:14 2008''
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Current revision

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF A THERMOPHILIC ENDOCELLULASE

PDB ID 1tml

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