1ogo

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[[Image:1ogo.gif|left|200px]]<br /><applet load="1ogo" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ogo, resolution 1.65&Aring;" />
 
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'''DEX49A FROM PENICILLIUM MINIOLUTEUM COMPLEX WITH ISOMALTOSE'''<br />
 
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==Overview==
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==Dex49A from Penicillium minioluteum complex with isomaltose==
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Dextranase catalyzes the hydrolysis of the alpha-1,6-glycosidic linkage in, dextran polymers. The structure of dextranase, Dex49A, from Penicillium, minioluteum was solved in the apo-enzyme and product-bound forms. The main, domain of the enzyme is a right-handed parallel beta helix, which is, connected to a beta sandwich domain at the N terminus. In the structure of, the product complex, isomaltose was found to bind in a crevice on the, surface of the enzyme. The glycosidic oxygen of the glucose unit in, subsite +1 forms a hydrogen bond to the suggested catalytic acid, Asp395., By NMR spectroscopy the reaction course was shown to occur with net, inversion at the anomeric carbon, implying a single displacement, mechanism. Both Asp376 and Asp396 are suitably positioned to activate the, water molecule that performs the nucleophilic attack. A new clan that, links glycoside hydrolase families 28 and 49 is suggested.
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<StructureSection load='1ogo' size='340' side='right'caption='[[1ogo]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ogo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Talaromyces_minioluteus Talaromyces minioluteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OGO FirstGlance]. <br>
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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]] 1.65&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr>
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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=1ogo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ogo OCA], [https://pdbe.org/1ogo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ogo RCSB], [https://www.ebi.ac.uk/pdbsum/1ogo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ogo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DEXT_TALMI DEXT_TALMI]
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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/og/1ogo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ogo 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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Dextranase catalyzes the hydrolysis of the alpha-1,6-glycosidic linkage in dextran polymers. The structure of dextranase, Dex49A, from Penicillium minioluteum was solved in the apo-enzyme and product-bound forms. The main domain of the enzyme is a right-handed parallel beta helix, which is connected to a beta sandwich domain at the N terminus. In the structure of the product complex, isomaltose was found to bind in a crevice on the surface of the enzyme. The glycosidic oxygen of the glucose unit in subsite +1 forms a hydrogen bond to the suggested catalytic acid, Asp395. By NMR spectroscopy the reaction course was shown to occur with net inversion at the anomeric carbon, implying a single displacement mechanism. Both Asp376 and Asp396 are suitably positioned to activate the water molecule that performs the nucleophilic attack. A new clan that links glycoside hydrolase families 28 and 49 is suggested.
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==About this Structure==
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Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex.,Larsson AM, Andersson R, Stahlberg J, Kenne L, Jones TA Structure. 2003 Sep;11(9):1111-21. PMID:12962629<ref>PMID:12962629</ref>
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1OGO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_minioluteum Penicillium minioluteum]. Active as [http://en.wikipedia.org/wiki/Dextranase Dextranase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.11 3.2.1.11] Known structural/functional Site: <scene name='pdbsite=CAT:Glc+Binding+Site+For+Chain+X'>CAT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGO OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex., Larsson AM, Andersson R, Stahlberg J, Kenne L, Jones TA, Structure. 2003 Sep;11(9):1111-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12962629 12962629]
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</div>
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[[Category: Dextranase]]
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<div class="pdbe-citations 1ogo" style="background-color:#fffaf0;"></div>
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[[Category: Penicillium minioluteum]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Jones, T.A.]]
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__TOC__
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[[Category: Larsson, A.M.]]
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</StructureSection>
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[[Category: Stahlberg, J.]]
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[[Category: Large Structures]]
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[[Category: dextran degradation]]
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[[Category: Talaromyces minioluteus]]
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[[Category: glycosidase]]
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[[Category: Jones TA]]
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[[Category: hydrolase]]
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[[Category: Larsson AM]]
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[[Category: Stahlberg J]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:57:52 2008''
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Current revision

Dex49A from Penicillium minioluteum complex with isomaltose

PDB ID 1ogo

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