1t0o: Difference between revisions

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New page: left|200px<br /><applet load="1t0o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t0o, resolution 1.96Å" /> '''The structure of alp...
 
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[[Image:1t0o.gif|left|200px]]<br /><applet load="1t0o" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1t0o.gif|left|200px]]<br /><applet load="1t0o" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1t0o, resolution 1.96&Aring;" />
caption="1t0o, resolution 1.96&Aring;" />
'''The structure of alpha-galactosidase from Trichoderma reesei complexed with beta-D-galactose'''<br />
'''The structure of alpha-galactosidase from Trichoderma reesei complexed with beta-D-galactose'''<br />


==Overview==
==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.
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==
==About this Structure==
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 GAL 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T0O OCA].  
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].  


==Reference==
==Reference==
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[[Category: Hypocrea jecorina]]
[[Category: Hypocrea jecorina]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Eneyskaya, E.V.]]
[[Category: Eneyskaya, E V.]]
[[Category: Golubev, A.M.]]
[[Category: Golubev, A M.]]
[[Category: Kulminskaya, A.A.]]
[[Category: Kulminskaya, A A.]]
[[Category: Nagem, R.A.P.]]
[[Category: Nagem, R A.P.]]
[[Category: Neto, J.R.Brandao.]]
[[Category: Neto, J R.Brandao.]]
[[Category: Neustroev, K.N.]]
[[Category: Neustroev, K N.]]
[[Category: Polikarpov, I.]]
[[Category: Polikarpov, I.]]
[[Category: Shabalin, K.A.]]
[[Category: Shabalin, K A.]]
[[Category: ev, A.N.Savel.]]
[[Category: ev, A N.Savel.]]
[[Category: GAL]]
[[Category: GAL]]
[[Category: (beta/alpha)8 barrel]]
[[Category: (beta/alpha)8 barrel]]
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[[Category: two domains]]
[[Category: two domains]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:33 2008''