2fv0: Difference between revisions

Line 1:

[[Image:2fv0.gif|left|200px]]<br /><applet load="2fv0" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2fv0.gif|left|200px]]<br /><applet load="2fv0" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2fv0, resolution 1.91Å" />

'''UGL_D88N/dGlcA-Glc-Rha-Glc'''<br />

==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.

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==

2FV0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2FV0 OCA].

2FV0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FV0 OCA].

==Reference==

Line 19:

[[Category: alpha6/alpha6-barrel]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 10:47:~~09 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:25:22 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2fv0.gif|left|200px]]<br /><applet load="2fv0" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2fv0.gif|left|200px]]<br /><applet load="2fv0" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2fv0, resolution 1.91&Aring;" />
 '''UGL_D88N/dGlcA-Glc-Rha-Glc'''<br />
 ==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.
+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==
-FV0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FV0 OCA].
+FV0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FV0 OCA].
 ==Reference==
@@ Line 19: / Line 19: @@
 [[Category: alpha6/alpha6-barrel]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:47:09 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:25:22 2008''