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2amg

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{{STRUCTURE_2amg| PDB=2amg | SCENE= }}
{{STRUCTURE_2amg| PDB=2amg | SCENE= }}
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'''STRUCTURE OF HYDROLASE (GLYCOSIDASE)'''
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===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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9126844 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9126844}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Signal]]
[[Category: Signal]]
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''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

Image:2amg.png

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

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