2fuz
From Proteopedia
(New page: 200px<br /><applet load="2fuz" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fuz, resolution 1.80Å" /> '''UGL hexagonal crysta...) |
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| - | [[Image:2fuz.gif|left|200px]]<br /><applet load="2fuz" size=" | + | [[Image:2fuz.gif|left|200px]]<br /><applet load="2fuz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fuz, resolution 1.80Å" /> | caption="2fuz, resolution 1.80Å" /> | ||
'''UGL hexagonal crystal structure without glycine and DTT molecules'''<br /> | '''UGL hexagonal crystal structure without glycine and DTT molecules'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacterial unsaturated glucuronyl hydrolases (UGLs) together with | + | Bacterial unsaturated glucuronyl hydrolases (UGLs) together with polysaccharide lyases are responsible for the complete depolymerization of mammalian extracellular matrix glycosaminoglycans. UGL acts on various oligosaccharides containing unsaturated glucuronic acid (DeltaGlcA) at the nonreducing terminus and releases DeltaGlcA through hydrolysis. In this study, we demonstrate the substrate recognition mechanism of the UGL of Bacillus sp. GL1 by determining the X-ray crystallographic structure of its substrate-enzyme complexes. The tetrasaccharide-enzyme complex demonstrated that at least four subsites are present in the active pocket. Although several amino acid residues are crucial for substrate binding, the enzyme strongly recognizes DeltaGlcA at subsite -1 through the formation of hydrogen bonds and stacking interactions, and prefers N-acetyl-d-galactosamine and glucose rather than N-acetyl-d-glucosamine as a residue accommodated in subsite +1, due to the steric hindrance. |
==About this Structure== | ==About this Structure== | ||
| - | 2FUZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with MPD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2FUZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: alpha6/alpha6-barrel]] | [[Category: alpha6/alpha6-barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:25:22 2008'' |
Revision as of 15:25, 21 February 2008
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UGL hexagonal crystal structure without glycine and DTT molecules
Overview
Bacterial unsaturated glucuronyl hydrolases (UGLs) together with polysaccharide lyases are responsible for the complete depolymerization of mammalian extracellular matrix glycosaminoglycans. UGL acts on various oligosaccharides containing unsaturated glucuronic acid (DeltaGlcA) at the nonreducing terminus and releases DeltaGlcA through hydrolysis. In this study, we demonstrate the substrate recognition mechanism of the UGL of Bacillus sp. GL1 by determining the X-ray crystallographic structure of its substrate-enzyme complexes. The tetrasaccharide-enzyme complex demonstrated that at least four subsites are present in the active pocket. Although several amino acid residues are crucial for substrate binding, the enzyme strongly recognizes DeltaGlcA at subsite -1 through the formation of hydrogen bonds and stacking interactions, and prefers N-acetyl-d-galactosamine and glucose rather than N-acetyl-d-glucosamine as a residue accommodated in subsite +1, due to the steric hindrance.
About this Structure
2FUZ is a Single protein structure of sequence from Bacillus sp. with as ligand. Full crystallographic information is available from OCA.
Reference
Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1., Itoh T, Hashimoto W, Mikami B, Murata K, Biochem Biophys Res Commun. 2006 May 26;344(1):253-62. PMID:16630576
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