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1t0o

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[[Image:1t0o.gif|left|200px]]<br /><applet load="1t0o" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1t0o.gif|left|200px]]
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caption="1t0o, resolution 1.96&Aring;" />
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'''The structure of alpha-galactosidase from Trichoderma reesei complexed with beta-D-galactose'''<br />
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{{Structure
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|PDB= 1t0o |SIZE=350|CAPTION= <scene name='initialview01'>1t0o</scene>, resolution 1.96&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</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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|GENE=
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}}
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'''The structure of alpha-galactosidase from Trichoderma reesei complexed with beta-D-galactose'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1T0O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina] with <scene name='pdbligand=GAL:'>GAL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0O OCA].
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1T0O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0O OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15136043 15136043]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15136043 15136043]
[[Category: Alpha-galactosidase]]
[[Category: Alpha-galactosidase]]
[[Category: Hypocrea jecorina]]
[[Category: Hypocrea jecorina]]
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[[Category: complex]]
[[Category: complex]]
[[Category: glycoprotein]]
[[Category: glycoprotein]]
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[[Category: two domains]]
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[[Category: two domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:12:06 2008''

Revision as of 12:12, 20 March 2008


PDB ID 1t0o

Drag the structure with the mouse to rotate
, resolution 1.96Å
Ligands:
Activity: Alpha-galactosidase, with EC number 3.2.1.22
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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