1uas
From Proteopedia
(New page: 200px<br /><applet load="1uas" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uas, resolution 1.50Å" /> '''Crystal structure of...) |
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| - | [[Image:1uas.jpg|left|200px]]<br /><applet load="1uas" size=" | + | [[Image:1uas.jpg|left|200px]]<br /><applet load="1uas" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uas, resolution 1.50Å" /> | caption="1uas, resolution 1.50Å" /> | ||
'''Crystal structure of rice alpha-galactosidase'''<br /> | '''Crystal structure of rice alpha-galactosidase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | alpha-Galactosidases catalyze the hydrolysis of alpha-1,6-linked | + | alpha-Galactosidases catalyze the hydrolysis of alpha-1,6-linked galactosyl residues from galacto-oligosaccharides and polymeric galacto-(gluco)mannans. The crystal structure of rice alpha-galactosidase has been determined at 1.5A resolution using the multiple isomorphous replacement method. The structure consisted of a catalytic domain and a C-terminal domain and was essentially the same as that of alpha-N-acetylgalactosaminidase, which is the same member of glycosyl hydrolase family 27. The catalytic domain had a (beta/alpha)8-barrel structure, and the C-terminal domain was made up of eight beta-strands containing a Greek key motif. The structure was solved as a complex with d-galactose, providing a mode of substrate binding in detail. The d-galactose molecule was found bound in the active site pocket on the C-terminal side of the central beta-barrel of the catalytic domain. The d-galactose molecule consisted of a mixture of two anomers present in a ratio equal to their natural abundance. Structural comparisons of rice alpha-galactosidase with chicken alpha-N-acetylgalactosaminidase provided further understanding of the substrate recognition mechanism in these enzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 1UAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa] with GLA, SO4, PT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-galactosidase Alpha-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.22 3.2.1.22] Full crystallographic information is available from [http:// | + | 1UAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa] with <scene name='pdbligand=GLA:'>GLA</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=PT:'>PT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-galactosidase Alpha-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.22 3.2.1.22] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UAS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tim-barrel]] | [[Category: tim-barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:22:27 2008'' |
Revision as of 13:22, 21 February 2008
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Crystal structure of rice alpha-galactosidase
Overview
alpha-Galactosidases catalyze the hydrolysis of alpha-1,6-linked galactosyl residues from galacto-oligosaccharides and polymeric galacto-(gluco)mannans. The crystal structure of rice alpha-galactosidase has been determined at 1.5A resolution using the multiple isomorphous replacement method. The structure consisted of a catalytic domain and a C-terminal domain and was essentially the same as that of alpha-N-acetylgalactosaminidase, which is the same member of glycosyl hydrolase family 27. The catalytic domain had a (beta/alpha)8-barrel structure, and the C-terminal domain was made up of eight beta-strands containing a Greek key motif. The structure was solved as a complex with d-galactose, providing a mode of substrate binding in detail. The d-galactose molecule was found bound in the active site pocket on the C-terminal side of the central beta-barrel of the catalytic domain. The d-galactose molecule consisted of a mixture of two anomers present in a ratio equal to their natural abundance. Structural comparisons of rice alpha-galactosidase with chicken alpha-N-acetylgalactosaminidase provided further understanding of the substrate recognition mechanism in these enzymes.
About this Structure
1UAS is a Single protein structure of sequence from Oryza sativa with , , and as ligands. Active as Alpha-galactosidase, with EC number 3.2.1.22 Full crystallographic information is available from OCA.
Reference
Crystal structure of rice alpha-galactosidase complexed with D-galactose., Fujimoto Z, Kaneko S, Momma M, Kobayashi H, Mizuno H, J Biol Chem. 2003 May 30;278(22):20313-8. Epub 2003 Mar 25. PMID:12657636
Page seeded by OCA on Thu Feb 21 15:22:27 2008
Categories: Alpha-galactosidase | Oryza sativa | Single protein | Fujimoto, Z. | Kaneko, S. | Kobayashi, H. | Mizuno, H. | Momma, M. | GLA | GOL | PT | SO4 | Beta-alpha-barrel | Greek key motif | Tim-barrel
