1ogo
From Proteopedia
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| - | [[Image:1ogo.gif|left|200px]] | + | [[Image:1ogo.gif|left|200px]] |
| - | + | ||
| - | '''DEX49A FROM PENICILLIUM MINIOLUTEUM COMPLEX WITH ISOMALTOSE''' | + | {{Structure |
| + | |PDB= 1ogo |SIZE=350|CAPTION= <scene name='initialview01'>1ogo</scene>, resolution 1.65Å | ||
| + | |SITE= <scene name='pdbsite=CAT:Glc+Binding+Site+For+Chain+X'>CAT</scene> | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''DEX49A FROM PENICILLIUM MINIOLUTEUM COMPLEX WITH ISOMALTOSE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OGO is a [ | + | 1OGO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_minioluteum Penicillium minioluteum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGO OCA]. |
==Reference== | ==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:[http:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/12962629 12962629] |
[[Category: Dextranase]] | [[Category: Dextranase]] | ||
[[Category: Penicillium minioluteum]] | [[Category: Penicillium minioluteum]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:10:36 2008'' |
Revision as of 11:10, 20 March 2008
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| , resolution 1.65Å | |||||||
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| Sites: | |||||||
| Activity: | Dextranase, with EC number 3.2.1.11 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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