1ogm

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[[Image:1ogm.gif|left|200px]]
[[Image:1ogm.gif|left|200px]]
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{{Structure
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|PDB= 1ogm |SIZE=350|CAPTION= <scene name='initialview01'>1ogm</scene>, resolution 1.80&Aring;
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The line below this paragraph, containing "STRUCTURE_1ogm", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=CAT:Catalytic+Residues'>CAT</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1ogm| PDB=1ogm | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ogm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ogm OCA], [http://www.ebi.ac.uk/pdbsum/1ogm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ogm RCSB]</span>
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'''DEX49A FROM PENICILLIUM MINIOLUTEUM'''
'''DEX49A FROM PENICILLIUM MINIOLUTEUM'''
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[[Category: Larsson, A M.]]
[[Category: Larsson, A M.]]
[[Category: Stahlberg, J.]]
[[Category: Stahlberg, J.]]
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[[Category: dextran degradation]]
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[[Category: Dextran degradation]]
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[[Category: glycosidase]]
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[[Category: Glycosidase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:49:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:45:00 2008''
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Revision as of 00:49, 3 May 2008

Image:1ogm.gif

Template:STRUCTURE 1ogm

DEX49A FROM PENICILLIUM MINIOLUTEUM


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

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 Page seeded by OCA on Sat May 3 03:49:14 2008

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