1qi3

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[[Image:1qi3.jpg|left|200px]]
[[Image:1qi3.jpg|left|200px]]
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{{Structure
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|PDB= 1qi3 |SIZE=350|CAPTION= <scene name='initialview01'>1qi3</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1qi3", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MTT:MALTOTETRAOSE'>MTT</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1qi3| PDB=1qi3 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qi3 OCA], [http://www.ebi.ac.uk/pdbsum/1qi3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qi3 RCSB]</span>
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}}
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'''MUTANT (D193N) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH MALTOTETRAOSE'''
'''MUTANT (D193N) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH MALTOTETRAOSE'''
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[[Category: Kubota, M.]]
[[Category: Kubota, M.]]
[[Category: Matsuura, Y.]]
[[Category: Matsuura, Y.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: maltotetraose-forming exo amylase]]
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[[Category: Maltotetraose-forming exo amylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:17:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:13:54 2008''
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Revision as of 03:18, 3 May 2008

Template:STRUCTURE 1qi3

MUTANT (D193N) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH MALTOTETRAOSE


Overview

The crystal structures of the four product-complexed single mutants of the catalytic residues of Pseudomonas stutzeri maltotetraose-forming alpha-amylase, E219G, D193N, D193G and D294N, have been determined. Possible roles of the catalytic residues Glu219, Asp193 and Asp294 have been discussed by comparing the structures among the previously determined complexed mutant E219Q and the present mutant enzymes. The results suggested that Asp193 predominantly works as the base catalyst (nucleophile), whose side chain atom lies in close proximity to the C1-atom of Glc4, being involved in the intermediate formation in the hydrolysis reaction. While Asp294 works for tightly binding the substrate to give a twisted and a deformed conformation of the glucose ring at position -1 (Glc4). The hydrogen bond between the side chain atom of Glu219 and the O1-atom of Glc4, that implies the possibility of interaction via hydrogen, consistently present throughout these analyses, supports the generally accepted role of this residue as the acid catalyst (proton donor).

About this Structure

1QI3 is a Single protein structure of sequence from Pseudomonas stutzeri. Full crystallographic information is available from OCA.

Reference

Roles of catalytic residues in alpha-amylases as evidenced by the structures of the product-complexed mutants of a maltotetraose-forming amylase., Hasegawa K, Kubota M, Matsuura Y, Protein Eng. 1999 Oct;12(10):819-24. PMID:10556241 Page seeded by OCA on Sat May 3 06:17:59 2008

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