1yoo: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==ASPARTATE AMINOTRANSFERASE MUTANT ATB17 WITH ISOVALERIC ACID== | ==ASPARTATE AMINOTRANSFERASE MUTANT ATB17 WITH ISOVALERIC ACID== | ||
<StructureSection load='1yoo' size='340' side='right' caption='[[1yoo]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1yoo' size='340' side='right'caption='[[1yoo]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1yoo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YOO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YOO FirstGlance]. <br> | <table><tr><td colspan='2'>[[1yoo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YOO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YOO FirstGlance]. <br> | ||
| Line 12: | Line 12: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yo/1yoo_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yo/1yoo_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 27: | Line 27: | ||
</div> | </div> | ||
<div class="pdbe-citations 1yoo" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1yoo" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 33: | Line 36: | ||
[[Category: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Aspartate transaminase]] | [[Category: Aspartate transaminase]] | ||
[[Category: Large Structures]] | |||
[[Category: Kagamiyama, H]] | [[Category: Kagamiyama, H]] | ||
[[Category: Okamoto, A]] | [[Category: Okamoto, A]] | ||
Revision as of 14:26, 4 December 2019
ASPARTATE AMINOTRANSFERASE MUTANT ATB17 WITH ISOVALERIC ACIDASPARTATE AMINOTRANSFERASE MUTANT ATB17 WITH ISOVALERIC ACID
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDirected 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||||