1ogo

<table><tr><td colspan='2'>[[1ogo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_137.84_[[penicillium_samsonii]] Cbs 137.84 [[penicillium samsonii]]]. 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>

</td></tr><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>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ogm|1ogm]]</div></td></tr>

<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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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ogo" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Dextranase]]

[[Category: Jones, T A]]

[[Category: Larsson, A M]]

[[Category: Stahlberg, J]]

[[Category: Dextran degradation]]

[[Category: Hydrolase]]