1szn: Difference between revisions

Revision as of 11:58, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1szn.png

Template:STRUCTURE 1szn

THE STRUCTURE OF ALPHA-GALACTOSIDASETHE STRUCTURE OF ALPHA-GALACTOSIDASE

Template:ABSTRACT PUBMED 15136043

About this StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 11:58:39 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1szn.gif|left|200px]]
+{{Seed}}
+[[Image:1szn.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1szn|  PDB=1szn  |  SCENE=  }}
-'''THE STRUCTURE OF ALPHA-GALACTOSIDASE'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15136043}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15136043 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15136043}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Ev, A N.Savel.]]
 [[Category: Glycoprotein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:19:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:58:39 2008''