1suc: Difference between revisions
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[[Image:1suc.jpg|left|200px]] | [[Image:1suc.jpg|left|200px]] | ||
'''CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN''' | {{Structure | ||
|PDB= 1suc |SIZE=350|CAPTION= <scene name='initialview01'>1suc</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=CYA:TWO+OXYGEN+ATOMS+BOUND+TO+SG+OF+CYS'>CYA</scene> and <scene name='pdbligand=ACN:ACETONE'>ACN</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SUC is a [ | 1SUC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUC OCA]. | ||
==Reference== | ==Reference== | ||
Calcium-independent subtilisin by design., Gallagher T, Bryan P, Gilliland GL, Proteins. 1993 Jun;16(2):205-13. PMID:[http:// | Calcium-independent subtilisin by design., Gallagher T, Bryan P, Gilliland GL, Proteins. 1993 Jun;16(2):205-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8332608 8332608] | ||
[[Category: Bacillus amyloliquefaciens]] | [[Category: Bacillus amyloliquefaciens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase(serine proteinase)]] | [[Category: hydrolase(serine proteinase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:09:44 2008'' |
Revision as of 15:09, 20 March 2008
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, resolution 1.8Å | |||||||
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Ligands: | , and | ||||||
Activity: | Subtilisin, with EC number 3.4.21.62 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN
OverviewOverview
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 StructureAbout this Structure
1SUC is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.
ReferenceReference
Calcium-independent subtilisin by design., Gallagher T, Bryan P, Gilliland GL, Proteins. 1993 Jun;16(2):205-13. PMID:8332608
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