1ob0: Difference between revisions
New page: left|200px<br /> <applet load="1ob0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ob0, resolution 1.83Å" /> '''KINETIC STABILIZATI... |
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==About this Structure== | ==About this Structure== | ||
1OB0 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]] with CA and NA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OB0 OCA]]. | 1OB0 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]] with CA and NA as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OB0 OCA]]. | ||
==Reference== | ==Reference== | ||
Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface., Machius M, Declerck N, Huber R, Wiegand G, J Biol Chem. 2003 Mar 28;278(13):11546-53. Epub 2003 Jan 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12540849 12540849] | Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface., Machius M, Declerck N, Huber R, Wiegand G, J Biol Chem. 2003 Mar 28;278(13):11546-53. Epub 2003 Jan 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12540849 12540849] | ||
[[Category: Alpha-amylase]] | |||
[[Category: Bacillus licheniformis]] | [[Category: Bacillus licheniformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thermostability]] | [[Category: thermostability]] | ||
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Revision as of 12:06, 30 October 2007
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KINETIC STABILIZATION OF BACILLUS LICHENIFORMIS-AMYLASE THROUGH INTRODUCTION OF HYDROPHOBIC RESIDUES AT THE SURFACE
OverviewOverview
It is generally assumed that in proteins hydrophobic residues are not, favorable at solvent-exposed sites, and that amino acid substitutions on, the surface have little effect on protein thermostability. Contrary to, these assumptions, we have identified hyperthermostable variants of, Bacillus licheniformis alpha-amylase (BLA) that result from the, incorporation of hydrophobic residues at the surface. Under highly, destabilizing conditions, a variant combining five stabilizing mutations, unfolds 32 times more slowly and at a temperature 13 degrees C higher than, the wild-type. Crystal structure analysis at 1.7 A resolution suggests, that stabilization is achieved through (a) extension of the concept of, increased hydrophobic packing, usually applied to cavities, to surface, indentations, ... [(full description)]
About this StructureAbout this Structure
1OB0 is a [Single protein] structure of sequence from [Bacillus licheniformis] with CA and NA as [ligands]. Active as [Alpha-amylase], with EC number [3.2.1.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface., Machius M, Declerck N, Huber R, Wiegand G, J Biol Chem. 2003 Mar 28;278(13):11546-53. Epub 2003 Jan 21. PMID:12540849
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