2aaa: Difference between revisions

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[[Image:2aaa.~~jpg~~|left|200px]]

[[Image:2aaa.png|left|200px]]

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~~'''~~CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION STUDY AT 2.1 ANGSTROMS RESOLUTION OF TWO ENZYMES FROM ASPERGILLUS~~'''~~

===CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION STUDY AT 2.1 ANGSTROMS RESOLUTION OF TWO ENZYMES FROM ASPERGILLUS===

~~==Overview==~~

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X-~~ray diffraction analysis (at 2.1~~-~~A resolution) of an acid alpha-amylase from Aspergillus niger allowed a detailed description of the stereochemistry of the calcium-binding sites.~~ The primary site (which is essential in maintaining proper folding around the active site) contains a tightly bound Ca2+ with an unusually high number of eight ligands (O delta 1 and O delta 2 of Asp175, O delta of Asn121, ~~main-chain carbonyl oxygens of Glu162 and Glu210~~, ~~and three water molecules). A secondary binding site was identified at~~ the ~~bottom of the substrate binding cleft; it involves the residues presumed~~ to ~~play a catalytic role (Asp206 and Glu230). This explains~~ the ~~inhibitory effect of calcium observed at higher concentrations. Neutral Aspergillus oryzae~~ (~~TAKA) alpha-amylase was also refined in a new crystal~~ at 2.~~1-A resolution~~. ~~The structure of this homologous (over 80%~~) ~~enzyme and additional kinetic studies support all~~ the ~~structural conclusions regarding both calcium~~-~~binding sites.~~

The line below this paragraph, {{ABSTRACT_PUBMED_2207069}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 2207069 is the PubMed ID number.

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==About this Structure==

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[[Category: Dodson, G G.]]

[[Category: Glycosidase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 18~~:48:36 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:04:32 2008''

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-[[Image:2aaa.jpg|left|200px]]
+{{Seed}}
+[[Image:2aaa.png|left|200px]]
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 {{STRUCTURE_2aaa|  PDB=2aaa  |  SCENE=  }}
-'''CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION STUDY AT 2.1 ANGSTROMS RESOLUTION OF TWO ENZYMES FROM ASPERGILLUS'''
+===CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION STUDY AT 2.1 ANGSTROMS RESOLUTION OF TWO ENZYMES FROM ASPERGILLUS===
-==Overview==
+<!--
-X-ray diffraction analysis (at 2.1-A resolution) of an acid alpha-amylase from Aspergillus niger allowed a detailed description of the stereochemistry of the calcium-binding sites. The primary site (which is essential in maintaining proper folding around the active site) contains a tightly bound Ca2+ with an unusually high number of eight ligands (O delta 1 and O delta 2 of Asp175, O delta of Asn121, main-chain carbonyl oxygens of Glu162 and Glu210, and three water molecules). A secondary binding site was identified at the bottom of the substrate binding cleft; it involves the residues presumed to play a catalytic role (Asp206 and Glu230). This explains the inhibitory effect of calcium observed at higher concentrations. Neutral Aspergillus oryzae (TAKA) alpha-amylase was also refined in a new crystal at 2.1-A resolution. The structure of this homologous (over 80%) enzyme and additional kinetic studies support all the structural conclusions regarding both calcium-binding sites.
+The line below this paragraph, {{ABSTRACT_PUBMED_2207069}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 2207069 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_2207069}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Dodson, G G.]]
 [[Category: Glycosidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:48:36 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:04:32 2008''