1yoo

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|PDB= 1yoo |SIZE=350|CAPTION= <scene name='initialview01'>1yoo</scene>, resolution 2.40&Aring;
|PDB= 1yoo |SIZE=350|CAPTION= <scene name='initialview01'>1yoo</scene>, resolution 2.40&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> and <scene name='pdbligand=IVA:ISOVALERIC ACID'>IVA</scene>
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|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene> and <scene name='pdbligand=IVA:ISOVALERIC ACID'>IVA</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1]
|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1]
|GENE=
|GENE=
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[[Category: aminotransferase]]
[[Category: aminotransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:25:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:22:49 2008''

Revision as of 12:22, 23 March 2008


PDB ID 1yoo

Drag the structure with the mouse to rotate
, resolution 2.40Å
Ligands: and
Activity: Aspartate transaminase, with EC number 2.6.1.1
Coordinates: save as pdb, mmCIF, xml



ASPARTATE AMINOTRANSFERASE MUTANT ATB17 WITH ISOVALERIC ACID


Overview

Directed evolution was used to change the substrate specificity of aspartate aminotransferase. A mutant enzyme with 17 amino acid substitutions was generated that shows a 2.1 x 10(6)-fold increase in the catalytic efficiency (kcat/Km) for a non-native substrate, valine. The absorption spectrum of the bound coenzyme, pyridoxal 5'-phosphate, is also changed significantly by the mutations. Interestingly, only one of the 17 residues appears to be able to contact the substrate, and none of them interact with the coenzyme. The three-dimensional structure of the mutant enzyme complexed with a valine analog, isovalerate (determined to 2.4-A resolution by x-ray crystallography), provides insights into how the mutations affect substrate binding. The active site is remodeled; the subunit interface is altered, and the enzyme domain that encloses the substrate is shifted by the mutations. The present results demonstrate clearly the importance of the cumulative effects of residues remote from the active site and represent a new line of approach to the redesign of enzyme activity.

About this Structure

1YOO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues., Oue S, Okamoto A, Yano T, Kagamiyama H, J Biol Chem. 1999 Jan 22;274(4):2344-9. PMID:9891001

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