1ulv
From Proteopedia
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| - | [[Image:1ulv.jpg|left|200px]] | + | [[Image:1ulv.jpg|left|200px]] |
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| - | '''Crystal Structure of Glucodextranase Complexed with Acarbose''' | + | {{Structure |
| + | |PDB= 1ulv |SIZE=350|CAPTION= <scene name='initialview01'>1ulv</scene>, resolution 2.42Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACR:ACARBOSE'>ACR</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Glucan_1,6-alpha-glucosidase Glucan 1,6-alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.70 3.2.1.70] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of Glucodextranase Complexed with Acarbose''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ULV is a [ | + | 1ULV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULV OCA]. |
==Reference== | ==Reference== | ||
| - | Structural insights into substrate specificity and function of glucodextranase., Mizuno M, Tonozuka T, Suzuki S, Uotsu-Tomita R, Kamitori S, Nishikawa A, Sakano Y, J Biol Chem. 2004 Mar 12;279(11):10575-83. Epub 2003 Dec 1. PMID:[http:// | + | Structural insights into substrate specificity and function of glucodextranase., Mizuno M, Tonozuka T, Suzuki S, Uotsu-Tomita R, Kamitori S, Nishikawa A, Sakano Y, J Biol Chem. 2004 Mar 12;279(11):10575-83. Epub 2003 Dec 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14660574 14660574] |
[[Category: Arthrobacter globiformis]] | [[Category: Arthrobacter globiformis]] | ||
[[Category: Glucan 1,6-alpha-glucosidase]] | [[Category: Glucan 1,6-alpha-glucosidase]] | ||
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[[Category: slh domain]] | [[Category: slh domain]] | ||
| - | ''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 14:33:48 2008'' |
Revision as of 12:33, 20 March 2008
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| , resolution 2.42Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Glucan 1,6-alpha-glucosidase, with EC number 3.2.1.70 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Glucodextranase Complexed with Acarbose
Overview
A glucodextranase (iGDase) from Arthrobacter globiformis I42 hydrolyzes alpha-1,6-glucosidic linkages of dextran from the non-reducing end to produce beta-D-glucose via an inverting reaction mechanism and classified into the glycoside hydrolase family 15 (GH15). Here we cloned the iGDase gene and determined the crystal structures of iGDase of the unliganded form and the complex with acarbose at 2.42-A resolution. The structure of iGDase is composed of four domains N, A, B, and C. Domain A forms an (alpha/alpha)(6)-barrel structure and domain N consists of 17 antiparallel beta-strands, and both domains are conserved in bacterial glucoamylases (GAs) and appear to be mainly concerned with catalytic activity. The structure of iGDase complexed with acarbose revealed that the positions and orientations of the residues at subsites -1 and +1 are nearly identical between iGDase and GA; however, the residues corresponding to subsite 3, which form the entrance of the substrate binding pocket, and the position of the open space and constriction of iGDase are different from those of GAs. On the other hand, domains B and C are not found in the bacterial GAs. The primary structure of domain C is homologous with a surface layer homology domain of pullulanases, and the three-dimensional structure of domain C resembles the carbohydrate-binding domain of some glycohydrolases.
About this Structure
1ULV is a Single protein structure of sequence from Arthrobacter globiformis. Full crystallographic information is available from OCA.
Reference
Structural insights into substrate specificity and function of glucodextranase., Mizuno M, Tonozuka T, Suzuki S, Uotsu-Tomita R, Kamitori S, Nishikawa A, Sakano Y, J Biol Chem. 2004 Mar 12;279(11):10575-83. Epub 2003 Dec 1. PMID:14660574
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