2amg
From Proteopedia
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|PDB= 2amg |SIZE=350|CAPTION= <scene name='initialview01'>2amg</scene>, resolution 2.0Å | |PDB= 2amg |SIZE=350|CAPTION= <scene name='initialview01'>2amg</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Glucan_1,4-alpha-maltotetraohydrolase Glucan 1,4-alpha-maltotetraohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.60 3.2.1.60] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucan_1,4-alpha-maltotetraohydrolase Glucan 1,4-alpha-maltotetraohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.60 3.2.1.60] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2amg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2amg OCA], [http://www.ebi.ac.uk/pdbsum/2amg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2amg RCSB]</span> | ||
}} | }} | ||
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[[Category: Morishita, Y.]] | [[Category: Morishita, Y.]] | ||
[[Category: Sakai, S.]] | [[Category: Sakai, S.]] | ||
| - | [[Category: CA]] | ||
[[Category: carbohydrate metabolism]] | [[Category: carbohydrate metabolism]] | ||
[[Category: glycosidase]] | [[Category: glycosidase]] | ||
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[[Category: signal]] | [[Category: signal]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:54:33 2008'' |
Revision as of 22:54, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Glucan 1,4-alpha-maltotetraohydrolase, with EC number 3.2.1.60 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF HYDROLASE (GLYCOSIDASE)
Overview
The three-dimensional structure of an exo-type alpha-amylase from Pseudomonas stutzeri which degrades starch from its non-reducing end to produce maltotetraose has been determined by X-ray structure analysis. The catalytic domain of this enzyme (G4-2), whose structure was determined, is a product of spontaneous limited proteolysis in culture broth. It has 429 amino acid residues and a molecular mass of 47,200, and crystallizes in ammonium sulfate solution at pH 7.5. The structure was elucidated by the multiple isomorphous replacement method and refined at 2.0 A resolution, resulting in a final R-factor of 0.178 for significant reflections with a root-mean-square deviation from ideality in bond distances of 0.013 A. The polypeptide chain of this molecule folds into three domains; the first with a (beta/alpha)8 barrel structure, the second with an excursed part from the first one, and the third with five-stranded antiparallel beta-sheets. The active cleft is formed on the C-terminal side of the beta-sheets in the (beta/alpha)8 barrel as in the known endo-type alpha-amylases. A histidine side-chain nitrogen ND1 is coordinated to one of the bound calcium ion. The recognition site of the non-reducing end of the amylose that determines exo-wise degradation is presumed to be at one end of this cleft where there is a disordered loop consisting of the 66th to 72nd residues, and a loop carrying an aspartic acid (Asp160). These structural features may be responsible for the binding of the non-reducing end of the substrate amylose.
About this Structure
2AMG is a Single protein structure of sequence from Pseudomonas stutzeri. This structure supersedes the now removed PDB entry 1AMG. Full crystallographic information is available from OCA.
Reference
Crystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri., Morishita Y, Hasegawa K, Matsuura Y, Katsube Y, Kubota M, Sakai S, J Mol Biol. 1997 Apr 4;267(3):661-72. PMID:9126844
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