1szn

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|PDB= 1szn |SIZE=350|CAPTION= <scene name='initialview01'>1szn</scene>, resolution 1.54&Aring;
|PDB= 1szn |SIZE=350|CAPTION= <scene name='initialview01'>1szn</scene>, resolution 1.54&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-galactosidase Alpha-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.22 3.2.1.22]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-galactosidase Alpha-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.22 3.2.1.22] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1szn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1szn OCA], [http://www.ebi.ac.uk/pdbsum/1szn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1szn RCSB]</span>
}}
}}
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[[Category: Shabalin, K A.]]
[[Category: Shabalin, K A.]]
[[Category: ev, A N.Savel.]]
[[Category: ev, A N.Savel.]]
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[[Category: GOL]]
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[[Category: (beta/alpha)8 barrel,two domain]]
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[[Category: (beta/alpha)8 barrel]]
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[[Category: glycoprotein]]
[[Category: glycoprotein]]
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[[Category: two domain]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:11:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:05 2008''

Revision as of 20:49, 30 March 2008


PDB ID 1szn

Drag the structure with the mouse to rotate
, resolution 1.54Å
Ligands: , , ,
Activity: Alpha-galactosidase, with EC number 3.2.1.22
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



THE STRUCTURE OF ALPHA-GALACTOSIDASE


Overview

The crystal structures of alpha-galactosidase from the mesophilic fungus Trichoderma reesei and its complex with the competitive inhibitor, beta-d-galactose, have been determined at 1.54 A and 2.0 A resolution, respectively. The alpha-galactosidase structure was solved by the quick cryo-soaking method using a single Cs derivative. The refined crystallographic model of the alpha-galactosidase consists of two domains, an N-terminal catalytic domain of the (beta/alpha)8 barrel topology and a C-terminal domain which is formed by an antiparallel beta-structure. The protein contains four N-glycosylation sites located in the catalytic domain. Some of the oligosaccharides were found to participate in inter-domain contacts. The galactose molecule binds to the active site pocket located in the center of the barrel of the catalytic domain. Analysis of the alpha-galactosidase- galactose complex reveals the residues of the active site and offers a structural basis for identification of the putative mechanism of the enzymatic reaction. The structure of the alpha-galactosidase closely resembles those of the glycoside hydrolase family 27. The conservation of two catalytic Asp residues, identified for this family, is consistent with a double-displacement reaction mechanism for the alpha-galactosidase. Modeling of possible substrates into the active site reveals specific hydrogen bonds and hydrophobic interactions that could explain peculiarities of the enzyme kinetics.

About this Structure

1SZN is a Single protein structure of sequence from Hypocrea jecorina. Full crystallographic information is available from OCA.

Reference

Crystal structure of alpha-galactosidase from Trichoderma reesei and its complex with galactose: implications for catalytic mechanism., Golubev AM, Nagem RA, Brandao Neto JR, Neustroev KN, Eneyskaya EV, Kulminskaya AA, Shabalin KA, Savel'ev AN, Polikarpov I, J Mol Biol. 2004 May 28;339(2):413-22. PMID:15136043

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