1sud
From Proteopedia
(New page: 200px<br /><applet load="1sud" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sud, resolution 1.9Å" /> '''CALCIUM-INDEPENDENT S...) |
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| - | [[Image:1sud.jpg|left|200px]]<br /><applet load="1sud" size=" | + | [[Image:1sud.jpg|left|200px]]<br /><applet load="1sud" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sud, resolution 1.9Å" /> | caption="1sud, resolution 1.9Å" /> | ||
'''CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN'''<br /> | '''CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A version of subtilisin BPN' lacking the high affinity calcium site (site | + | A version of subtilisin BPN' lacking the high affinity calcium site (site A) has been produced through genetic engineering methods, and its crystal structure refined at 1.8 A resolution. This protein and the corresponding version containing the calcium A site are described and compared. The deletion of residues 75-83 was made in the context of four site-specific replacements previously shown to stabilize subtilisin. The helix that in wild type is interrupted by the calcium binding loop, is continuous in the deletion mutant, with normal geometry. A few residues adjacent to the loop, principally those that were involved in calcium coordination, are repositioned and/or destabilized by the deletion. Because refolding is greatly facilitated by the absence of the Ca-loop, this protein offers a new vehicle for analysis and dissection of the folding reaction. This is among the largest internal changes to a protein to be described at atomic resolution. |
==About this Structure== | ==About this Structure== | ||
| - | 1SUD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] with CA, K, CYA and ACN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http:// | + | 1SUD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=CYA:'>CYA</scene> and <scene name='pdbligand=ACN:'>ACN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bryan, P.]] | [[Category: Bryan, P.]] | ||
[[Category: Gallagher, T.]] | [[Category: Gallagher, T.]] | ||
| - | [[Category: Gilliland, G | + | [[Category: Gilliland, G L.]] |
[[Category: ACN]] | [[Category: ACN]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: hydrolase(serine proteinase)]] | [[Category: hydrolase(serine proteinase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:15 2008'' |
Revision as of 13:05, 21 February 2008
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CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN
Overview
A version of subtilisin BPN' lacking the high affinity calcium site (site A) has been produced through genetic engineering methods, and its crystal structure refined at 1.8 A resolution. This protein and the corresponding version containing the calcium A site are described and compared. The deletion of residues 75-83 was made in the context of four site-specific replacements previously shown to stabilize subtilisin. The helix that in wild type is interrupted by the calcium binding loop, is continuous in the deletion mutant, with normal geometry. A few residues adjacent to the loop, principally those that were involved in calcium coordination, are repositioned and/or destabilized by the deletion. Because refolding is greatly facilitated by the absence of the Ca-loop, this protein offers a new vehicle for analysis and dissection of the folding reaction. This is among the largest internal changes to a protein to be described at atomic resolution.
About this Structure
1SUD is a Single protein structure of sequence from Bacillus amyloliquefaciens with , , and as ligands. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
Reference
Calcium-independent subtilisin by design., Gallagher T, Bryan P, Gilliland GL, Proteins. 1993 Jun;16(2):205-13. PMID:8332608
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