2djm
From Proteopedia
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| - | [[Image:2djm.gif|left|200px]] | + | [[Image:2djm.gif|left|200px]] |
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| - | '''Solution structure of N-terminal starch-binding domain of glucoamylase from Rhizopus oryzae''' | + | {{Structure |
| + | |PDB= 2djm |SIZE=350|CAPTION= <scene name='initialview01'>2djm</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= amyA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=64495 Rhizopus oryzae]) | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of N-terminal starch-binding domain of glucoamylase from Rhizopus oryzae''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2DJM is a [ | + | 2DJM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhizopus_oryzae Rhizopus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DJM OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structure of family 21 carbohydrate-binding module from Rhizopus oryzae glucoamylase., Liu YN, Lai YT, Chou WI, Chang MD, Lyu PC, Biochem J. 2007 Apr 1;403(1):21-30. PMID:[http:// | + | Solution structure of family 21 carbohydrate-binding module from Rhizopus oryzae glucoamylase., Liu YN, Lai YT, Chou WI, Chang MD, Lyu PC, Biochem J. 2007 Apr 1;403(1):21-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17117925 17117925] |
[[Category: Rhizopus oryzae]] | [[Category: Rhizopus oryzae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: strach binding]] | [[Category: strach binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:27:55 2008'' |
Revision as of 14:27, 20 March 2008
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| Gene: | amyA (Rhizopus oryzae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of N-terminal starch-binding domain of glucoamylase from Rhizopus oryzae
Overview
CBMs (carbohydrate-binding modules) function independently to assist carbohydrate-active enzymes. Family 21 CBMs contain approx. 100 amino acid residues, and some members have starchbinding functions or glycogen-binding activities. We report here the first structure of a family 21 CBM from the SBD (starch-binding domain) of Rhizopus oryzae glucoamylase (RoCBM21) determined by NMR spectroscopy. This CBM has a beta-sandwich fold with an immunoglobulin-like structure. Ligand-binding properties of RoCBM21 were analysed by chemical-shift perturbations and automated docking. Structural comparisons with previously reported SBDs revealed two types of topologies, namely type I and type II, with CBM20, CBM25, CBM26 and CBM41 showing type I topology, with CBM21 and CBM34 showing type II topology. According to the chemical-shift perturbations, RoCBM21 contains two ligand-binding sites. Residues in site II are similar to those found in the family 20 CBM from Aspergillus niger glucoamylase (AnCBM20). Site I, however, is embedded in a region with unique sequence motifs only found in some members of CBM21s. Additionally, docking of beta-cyclodextrin and malto-oligosaccharides highlights that side chains of Y83 and W47 (one-letter amino acid code) form the central part of the conserved binding platform in the SBD. The structure of RoCBM21 provides the first direct evidence of the structural features and the basis for protein-carbohydrate recognition from an SBD of CBM21.
About this Structure
2DJM is a Single protein structure of sequence from Rhizopus oryzae. Full crystallographic information is available from OCA.
Reference
Solution structure of family 21 carbohydrate-binding module from Rhizopus oryzae glucoamylase., Liu YN, Lai YT, Chou WI, Chang MD, Lyu PC, Biochem J. 2007 Apr 1;403(1):21-30. PMID:17117925
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