1jf5

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[[Image:1jf5.gif|left|200px]]
[[Image:1jf5.gif|left|200px]]
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{{Structure
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|PDB= 1jf5 |SIZE=350|CAPTION= <scene name='initialview01'>1jf5</scene>, resolution 3.20&Aring;
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The line below this paragraph, containing "STRUCTURE_1jf5", 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>
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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/Neopullulanase Neopullulanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.135 3.2.1.135] </span>
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{{STRUCTURE_1jf5| PDB=1jf5 | SCENE= }}
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|RELATEDENTRY=[[1bvz|1BVZ]], [[1jf6|1JF6]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jf5 OCA], [http://www.ebi.ac.uk/pdbsum/1jf5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jf5 RCSB]</span>
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'''CRYSTAL STRUCTURE OF THERMOACTINOMYCES VULGARIS R-47 ALPHA-AMYLASE 2 MUTANT F286A'''
'''CRYSTAL STRUCTURE OF THERMOACTINOMYCES VULGARIS R-47 ALPHA-AMYLASE 2 MUTANT F286A'''
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[[Category: Shimura, Y.]]
[[Category: Shimura, Y.]]
[[Category: Tonozuka, T.]]
[[Category: Tonozuka, T.]]
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[[Category: beta/alpha barrel]]
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[[Category: Beta/alpha barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:09:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:32:49 2008''
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Revision as of 18:09, 2 May 2008

Image:1jf5.gif

Template:STRUCTURE 1jf5

CRYSTAL STRUCTURE OF THERMOACTINOMYCES VULGARIS R-47 ALPHA-AMYLASE 2 MUTANT F286A


Overview

Phe286 located in the center of the active site of alpha-amylase 2 from Thermoactinomyces vulgaris R-47 (TVAII) plays an important role in the substrate recognition for cyclomaltooligosaccharides (cyclodextrins). The X-ray structures of mutant TVAIIs with the replacement of Phe286 by Ala (F286A) and Tyr (F286Y) were determined at 3.2 A resolution. Their structures have no significant differences from that of the wild-type enzyme. The kinetic analyses of Phe286-replaced variants showed that the variants with non-aromatic residues, Ala (F286A) and Leu (F286L), have lower enzymatic activities than those with aromatic residues, Tyr (F286Y) and Trp (F286W), and the replacement of Phe286 affects enzymatic activities for CDs more than those for starch.

About this Structure

1JF5 is a Single protein structure of sequence from Thermoactinomyces vulgaris. Full crystallographic information is available from OCA.

Reference

Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs., Ohtaki A, Kondo S, Shimura Y, Tonozuka T, Sakano Y, Kamitori S, Carbohydr Res. 2001 Sep 7;334(4):309-13. PMID:11527532 Page seeded by OCA on Fri May 2 21:09:01 2008

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