1ogm: Difference between revisions

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[[Image:1ogm.gif|left|200px]]
{{Seed}}
[[Image:1ogm.png|left|200px]]


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{{STRUCTURE_1ogm|  PDB=1ogm  |  SCENE=  }}  
{{STRUCTURE_1ogm|  PDB=1ogm  |  SCENE=  }}  


'''DEX49A FROM PENICILLIUM MINIOLUTEUM'''
===DEX49A FROM PENICILLIUM MINIOLUTEUM===




==Overview==
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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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{{ABSTRACT_PUBMED_12962629}}


==About this Structure==
==About this Structure==
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[[Category: Glycosidase]]
[[Category: Glycosidase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:53:37 2008''

Revision as of 21:53, 28 July 2008

File:1ogm.png

Template:STRUCTURE 1ogm

DEX49A FROM PENICILLIUM MINIOLUTEUM

Template:ABSTRACT PUBMED 12962629

About this Structure

1OGM is a Single protein structure of sequence from Penicillium minioluteum. 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

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