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| - | [[Image:2amg.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2amg| PDB=2amg | SCENE= }} | | {{STRUCTURE_2amg| PDB=2amg | SCENE= }} |
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| - | '''STRUCTURE OF HYDROLASE (GLYCOSIDASE)'''
| + | ===STRUCTURE OF HYDROLASE (GLYCOSIDASE)=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9126844}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9126844 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9126844}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| | [[Category: Signal]] | | [[Category: Signal]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:13:10 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:33:20 2008'' |
Revision as of 17:33, 27 July 2008
Template:STRUCTURE 2amg
STRUCTURE OF HYDROLASE (GLYCOSIDASE)
Template:ABSTRACT PUBMED 9126844
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
Page seeded by OCA on Sun Jul 27 20:33:20 2008
