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| - | [[Image:1x39.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1x39| PDB=1x39 | SCENE= }} | | {{STRUCTURE_1x39| PDB=1x39 | SCENE= }} |
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| - | '''Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme exo1 in complex with gluco-phenylimidazole'''
| + | ===Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme exo1 in complex with gluco-phenylimidazole=== |
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| - | ==Overview==
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| - | The interactions of a transition state mimic anilinomethyl glucoimidazole (AmGlcIm), with a K(i) constant of 0.6 x 10(-)(9) M and a Gibbs free energy value of -53.5 kJ/mol, with a family GH3 beta-d-glucan glucohydrolase from barley have been analyzed crystallographically and by ab initio quantum mechanical modeling. AmGlcIm binds 3 times more tightly to the beta-d-glucan glucohydrolase than a previously investigated phenyl glucoimidazole. In the enzyme-AmGlcIm complex, an additional residue, Tyr253, and a water molecule positioned between subsites -1 and +1 are recruited for binding. Analyses of the two binary complexes reveal the following. (i) An intricate network exists in which hydrogen bonds between the enzyme's catalytic pocket residues Lys206, His207, Tyr253, Asp285, and Glu491 and the glucoimidazoles are shorter by 0.15-0.53 A, compared with distances of hydrogen bonds in the Michaelis complex. (ii) The "glucose" moiety of the glucoimidazoles adopts a (4)E conformation that is vital for the low-nanomolar binding. (iii) The N1 atoms of the glucoimidazoles are positioned nearly optimally for in-line protonation by the Oepsilon1 atom of the catalytic acid/base Glu491. (iv) The enzyme derives binding energies from both glycone and aglycone components of the glucoimidazoles. (iv) The prevalent libration motion of the two domains of the enzyme could play a significant role during induced fit closure in the active site. (v) Modeling based on the structural data predicts that protons could be positioned on the N1 atoms of the glucoimidazoles, and the catalytic acid/base Glu491 could carry an overall negative charge. (vi) The enzyme-AmGlcIm complex reveals the likely structure of an early transition state during hydrolysis. Finally, the high-resolution structures enabled us to define minimal structures of oligosaccharides attached to Asn221, Asn498, and Asn600 N-glycosylation sites. | + | The line below this paragraph, {{ABSTRACT_PUBMED_16342944}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16342944 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16342944}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: 2-domain fold]] | | [[Category: 2-domain fold]] |
| | [[Category: Ligand-protein complex]] | | [[Category: Ligand-protein complex]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:28:21 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:09:30 2008'' |
Revision as of 16:09, 28 July 2008
Template:STRUCTURE 1x39
Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme exo1 in complex with gluco-phenylimidazole
Template:ABSTRACT PUBMED 16342944
About this Structure
1X39 is a Single protein structure of sequence from Hordeum vulgare. Full crystallographic information is available from OCA.
Reference
Structural rationale for low-nanomolar binding of transition state mimics to a family GH3 beta-D-glucan glucohydrolase from barley., Hrmova M, Streltsov VA, Smith BJ, Vasella A, Varghese JN, Fincher GB, Biochemistry. 2005 Dec 20;44(50):16529-39. PMID:16342944
Page seeded by OCA on Mon Jul 28 19:09:30 2008
