2taa
From Proteopedia
(New page: 200px<br /> <applet load="2taa" size="450" color="white" frame="true" align="right" spinBox="true" caption="2taa, resolution 3.0Å" /> '''STRUCTURE AND POSSIB...) |
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| - | [[Image:2taa.gif|left|200px]]<br /> | + | [[Image:2taa.gif|left|200px]]<br /><applet load="2taa" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2taa" size=" | + | |
caption="2taa, resolution 3.0Å" /> | caption="2taa, resolution 3.0Å" /> | ||
'''STRUCTURE AND POSSIBLE CATALYTIC RESIDUES OF TAKA-AMYLASE A'''<br /> | '''STRUCTURE AND POSSIBLE CATALYTIC RESIDUES OF TAKA-AMYLASE A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A complete molecular model of Taka-amylase A consisting of 478 amino acid | + | A complete molecular model of Taka-amylase A consisting of 478 amino acid residues was built with the aid of amino acid sequence data. Some typical structural features of the molecule are described. A model fitting of an amylose chain in the catalytic site of the enzyme showed a possible productive binding mode between substrate and enzyme. On the basis of the difference Fourier analysis and the model fitting study, glutamic acid (Glu230) and aspartic acid (Asp297), which are located at the bottom of the cleft, were concluded to be the catalytic residues, serving as the general acid and base, respectively. |
==About this Structure== | ==About this Structure== | ||
| - | 2TAA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 2TAA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1TAA. The following page contains interesting information on the relation of 2TAA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb74_1.html Alpha-amylase]]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TAA OCA]. |
==Reference== | ==Reference== | ||
| - | Structure and possible catalytic residues of Taka-amylase A., Matsuura Y, Kusunoki M, Harada W, Kakudo M, J Biochem | + | Structure and possible catalytic residues of Taka-amylase A., Matsuura Y, Kusunoki M, Harada W, Kakudo M, J Biochem. 1984 Mar;95(3):697-702. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=6609921 6609921] |
[[Category: Alpha-amylase]] | [[Category: Alpha-amylase]] | ||
[[Category: Aspergillus oryzae]] | [[Category: Aspergillus oryzae]] | ||
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[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:49:32 2008'' |
Revision as of 16:49, 21 February 2008
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STRUCTURE AND POSSIBLE CATALYTIC RESIDUES OF TAKA-AMYLASE A
Overview
A complete molecular model of Taka-amylase A consisting of 478 amino acid residues was built with the aid of amino acid sequence data. Some typical structural features of the molecule are described. A model fitting of an amylose chain in the catalytic site of the enzyme showed a possible productive binding mode between substrate and enzyme. On the basis of the difference Fourier analysis and the model fitting study, glutamic acid (Glu230) and aspartic acid (Asp297), which are located at the bottom of the cleft, were concluded to be the catalytic residues, serving as the general acid and base, respectively.
About this Structure
2TAA is a Single protein structure of sequence from Aspergillus oryzae with as ligand. This structure supersedes the now removed PDB entry 1TAA. The following page contains interesting information on the relation of 2TAA with [Alpha-amylase]. Active as Alpha-amylase, with EC number 3.2.1.1 Full crystallographic information is available from OCA.
Reference
Structure and possible catalytic residues of Taka-amylase A., Matsuura Y, Kusunoki M, Harada W, Kakudo M, J Biochem. 1984 Mar;95(3):697-702. PMID:6609921
Page seeded by OCA on Thu Feb 21 18:49:32 2008
