1ogm

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<StructureSection load='1ogm' size='340' side='right'caption='[[1ogm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1ogm' size='340' side='right'caption='[[1ogm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1ogm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_642.68 Cbs 642.68]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OGM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1ogm]] 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=1OGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OGM FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ogo|1ogo]]</div></td></tr>
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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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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dextranase Dextranase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.11 3.2.1.11] </span></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=1ogm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ogm OCA], [https://pdbe.org/1ogm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ogm RCSB], [https://www.ebi.ac.uk/pdbsum/1ogm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ogm ProSAT]</span></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=1ogm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ogm OCA], [https://pdbe.org/1ogm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ogm RCSB], [https://www.ebi.ac.uk/pdbsum/1ogm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ogm ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DEXT_TALMI DEXT_TALMI]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1ogm ConSurf].
</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=1ogm ConSurf].
<div style="clear:both"></div>
<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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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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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 1ogm" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cbs 642 68]]
 
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[[Category: Dextranase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Jones, T A]]
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[[Category: Talaromyces minioluteus]]
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[[Category: Larsson, A M]]
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[[Category: Jones TA]]
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[[Category: Stahlberg, J]]
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[[Category: Larsson AM]]
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[[Category: Dextran degradation]]
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[[Category: Stahlberg J]]
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[[Category: Glycosidase]]
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[[Category: Hydrolase]]
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Revision as of 05:47, 17 April 2024

Dex49A from Penicillium minioluteum

PDB ID 1ogm

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