1ogo
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1ogo.gif|left|200px]]<br /><applet load="1ogo" size=" | + | [[Image:1ogo.gif|left|200px]]<br /><applet load="1ogo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ogo, resolution 1.65Å" /> | caption="1ogo, resolution 1.65Å" /> | ||
'''DEX49A FROM PENICILLIUM MINIOLUTEUM COMPLEX WITH ISOMALTOSE'''<br /> | '''DEX49A FROM PENICILLIUM MINIOLUTEUM COMPLEX WITH ISOMALTOSE'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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]. |
==Reference== | ==Reference== | ||
| Line 21: | Line 21: | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:57:52 2008'' |
Revision as of 07:57, 3 February 2008
|
DEX49A FROM PENICILLIUM MINIOLUTEUM COMPLEX WITH ISOMALTOSE
Overview
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.
About this Structure
1OGO is a Single protein structure of sequence from Penicillium minioluteum. Active as Dextranase, with EC number 3.2.1.11 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Feb 3 09:57:52 2008
