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2aaa

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[[Image:2aaa.jpg|left|200px]]
[[Image:2aaa.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2aaa |SIZE=350|CAPTION= <scene name='initialview01'>2aaa</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_2aaa", 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/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] </span>
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_2aaa| PDB=2aaa | 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=2aaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aaa OCA], [http://www.ebi.ac.uk/pdbsum/2aaa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2aaa RCSB]</span>
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}}
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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'''
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[[Category: Dodson, E J.]]
[[Category: Dodson, E J.]]
[[Category: Dodson, G G.]]
[[Category: Dodson, G G.]]
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[[Category: glycosidase]]
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[[Category: Glycosidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:48:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:49:59 2008''
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Revision as of 15:48, 3 May 2008

Image:2aaa.jpg

Template:STRUCTURE 2aaa

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.

About this Structure

2AAA is a Single protein structure of sequence from Aspergillus niger. Full crystallographic information is available from OCA.

Reference

Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus., Boel E, Brady L, Brzozowski AM, Derewenda Z, Dodson GG, Jensen VJ, Petersen SB, Swift H, Thim L, Woldike HF, Biochemistry. 1990 Jul 3;29(26):6244-9. PMID:2207069 Page seeded by OCA on Sat May 3 18:48:36 2008

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