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| - | [[Image:1e55.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1e55| PDB=1e55 | SCENE= }} | | {{STRUCTURE_1e55| PDB=1e55 | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE ZMGLUE191D IN COMPLEX WITH THE COMPETITIVE INHIBITOR DHURRIN'''
| + | ===CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE ZMGLUE191D IN COMPLEX WITH THE COMPETITIVE INHIBITOR DHURRIN=== |
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| - | ==Overview==
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| - | The mechanism and the site of substrate (i.e., aglycone) recognition and specificity were investigated in maize beta-glucosidase (Glu1) by x-ray crystallography by using crystals of a catalytically inactive mutant (Glu1E191D) in complex with the natural substrate 2-O-beta-d-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOAGlc), the free aglycone DIMBOA, and competitive inhibitor para-hydroxy-S-mandelonitrile beta-glucoside (dhurrin). The structures of these complexes and of the free enzyme were solved at 2.1-, 2.1-, 2.0-, and 2.2-A resolution, respectively. The structural data from the complexes allowed us to visualize an intact substrate, free aglycone, or a competitive inhibitor in the slot-like active site of a beta-glucosidase. These data show that the aglycone moiety of the substrate is sandwiched between W378 on one side and F198, F205, and F466 on the other. Thus, specific conformations of these four hydrophobic amino acids and the shape of the aglycone-binding site they form determine aglycone recognition and substrate specificity in Glu1. In addition to these four residues, A467 interacts with the 7-methoxy group of DIMBOA. All residues but W378 are variable among beta-glucosidases that differ in substrate specificity, supporting the conclusion that these sites are the basis of aglycone recognition and binding (i.e., substrate specificity) in beta-glucosidases. The data also provide a plausible explanation for the competitive binding of dhurrin to maize beta-glucosidases with high affinity without being hydrolyzed.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11106394}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11106394 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11106394}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Inactive mutant e191d]] | | [[Category: Inactive mutant e191d]] |
| | [[Category: Retention of the anomeric configuration]] | | [[Category: Retention of the anomeric configuration]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:40:26 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:09:48 2008'' |
Revision as of 21:09, 30 June 2008
Template:STRUCTURE 1e55
CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE ZMGLUE191D IN COMPLEX WITH THE COMPETITIVE INHIBITOR DHURRIN
Template:ABSTRACT PUBMED 11106394
About this Structure
1E55 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
The mechanism of substrate (aglycone) specificity in beta -glucosidases is revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes., Czjzek M, Cicek M, Zamboni V, Bevan DR, Henrissat B, Esen A, Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13555-60. PMID:11106394
Page seeded by OCA on Tue Jul 1 00:09:48 2008
