1aq0
From Proteopedia
(New page: 200px<br /><applet load="1aq0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aq0, resolution 2.0Å" /> '''BARLEY 1,3-1,4-BETA-G...) |
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| - | [[Image:1aq0.jpg|left|200px]]<br /><applet load="1aq0" size=" | + | [[Image:1aq0.jpg|left|200px]]<br /><applet load="1aq0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1aq0, resolution 2.0Å" /> | caption="1aq0, resolution 2.0Å" /> | ||
'''BARLEY 1,3-1,4-BETA-GLUCANASE IN MONOCLINIC SPACE GROUP'''<br /> | '''BARLEY 1,3-1,4-BETA-GLUCANASE IN MONOCLINIC SPACE GROUP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Both plants and bacteria produce enzymes capable of degrading the | + | Both plants and bacteria produce enzymes capable of degrading the mixed-linked beta-glucan of the endosperm cell walls of cereal grains. The enzymes share the specificity for beta-1,4 glycosyl bonds of O-3-substituted glucose units in linear polysaccharides and a similar cleavage mechanism but are unrelated in sequence and tertiary structure. The three-dimensional structure of the 1,3-1, 4-beta-glucanase isoenzyme EII from barley was determined from monoclinic crystals at a resolution of 2.0 A. The protein is folded into a betaalpha8 barrel structure as has been shown previously (Varghese, J. N., Garrett, T. P. J., Colman, P. M., Chen, L., Hoj, P. B., and Fincher, G. B. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 2785-2789) by diffraction analysis at lower resolution of tetragonal crystals. It contains one N-glycosylation site which is described in detail with the sugar moieties attached to residue Asn190. The geometry and hydration of the barley 1,3-1,4-beta-glucanase is analyzed; a model beta-glucan fragment is placed into the binding site by molecular dynamics simulation, and the beta-glucan binding grooves of the plant and bacterial enzymes are compared. Their active sites are shown to have a small number of common features in generally dissimilar geometries that serve to explain both the identical substrate specificity and the observed differences in inhibitor binding. |
==About this Structure== | ==About this Structure== | ||
| - | 1AQ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] Full crystallographic information is available from [http:// | + | 1AQ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQ0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Heinemann, U.]] | [[Category: Heinemann, U.]] | ||
| - | [[Category: Mueller, J | + | [[Category: Mueller, J J.]] |
| - | [[Category: Thomsen, K | + | [[Category: Thomsen, K K.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
| Line 23: | Line 23: | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:47:08 2008'' |
Revision as of 09:47, 21 February 2008
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BARLEY 1,3-1,4-BETA-GLUCANASE IN MONOCLINIC SPACE GROUP
Overview
Both plants and bacteria produce enzymes capable of degrading the mixed-linked beta-glucan of the endosperm cell walls of cereal grains. The enzymes share the specificity for beta-1,4 glycosyl bonds of O-3-substituted glucose units in linear polysaccharides and a similar cleavage mechanism but are unrelated in sequence and tertiary structure. The three-dimensional structure of the 1,3-1, 4-beta-glucanase isoenzyme EII from barley was determined from monoclinic crystals at a resolution of 2.0 A. The protein is folded into a betaalpha8 barrel structure as has been shown previously (Varghese, J. N., Garrett, T. P. J., Colman, P. M., Chen, L., Hoj, P. B., and Fincher, G. B. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 2785-2789) by diffraction analysis at lower resolution of tetragonal crystals. It contains one N-glycosylation site which is described in detail with the sugar moieties attached to residue Asn190. The geometry and hydration of the barley 1,3-1,4-beta-glucanase is analyzed; a model beta-glucan fragment is placed into the binding site by molecular dynamics simulation, and the beta-glucan binding grooves of the plant and bacterial enzymes are compared. Their active sites are shown to have a small number of common features in generally dissimilar geometries that serve to explain both the identical substrate specificity and the observed differences in inhibitor binding.
About this Structure
1AQ0 is a Single protein structure of sequence from Hordeum vulgare with as ligand. Active as Licheninase, with EC number 3.2.1.73 Full crystallographic information is available from OCA.
Reference
Crystal structure of barley 1,3-1,4-beta-glucanase at 2.0-A resolution and comparison with Bacillus 1,3-1,4-beta-glucanase., Muller JJ, Thomsen KK, Heinemann U, J Biol Chem. 1998 Feb 6;273(6):3438-46. PMID:9452466
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