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New page: left|200px<br /><applet load="1jf5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jf5, resolution 3.20Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1jf5.gif|left|200px]]<br /><applet load="1jf5" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1jf5.gif|left|200px]]<br /><applet load="1jf5" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1jf5, resolution 3.20&Aring;" />
caption="1jf5, resolution 3.20&Aring;" />
'''CRYSTAL STRUCTURE OF THERMOACTINOMYCES VULGARIS R-47 ALPHA-AMYLASE 2 MUTANT F286A'''<br />
'''CRYSTAL STRUCTURE OF THERMOACTINOMYCES VULGARIS R-47 ALPHA-AMYLASE 2 MUTANT F286A'''<br />


==Overview==
==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.
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==
==About this Structure==
1JF5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JF5 OCA].  
1JF5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JF5 OCA].  


==Reference==
==Reference==
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[[Category: beta/alpha barrel]]
[[Category: beta/alpha barrel]]


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