1t0o: Difference between revisions
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|PDB= 1t0o |SIZE=350|CAPTION= <scene name='initialview01'>1t0o</scene>, resolution 1.96Å | |PDB= 1t0o |SIZE=350|CAPTION= <scene name='initialview01'>1t0o</scene>, resolution 1.96Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene> | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
|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] | |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= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1szn|1SZN]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0o OCA], [http://www.ebi.ac.uk/pdbsum/1t0o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t0o RCSB]</span> | |||
}} | }} | ||
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[[Category: Shabalin, K A.]] | [[Category: Shabalin, K A.]] | ||
[[Category: ev, A N.Savel.]] | [[Category: ev, A N.Savel.]] | ||
[[Category: (beta/alpha)8 barrel,two domain]] | |||
[[Category: (beta/alpha)8 barrel]] | |||
[[Category: beta-d-galactose]] | [[Category: beta-d-galactose]] | ||
[[Category: complex | [[Category: glycoprotein,complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:32 2008'' | ||
Revision as of 20:49, 30 March 2008
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| 1t0o, resolution 1.96Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | BMA, GAL, MAN, NAG | ||||||||||||
| Activity: | Alpha-galactosidase, with EC number 3.2.1.22 | ||||||||||||
| Related: | 1SZN
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
The structure of alpha-galactosidase from Trichoderma reesei complexed with beta-D-galactose
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
1T0O 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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