1suc: Difference between revisions
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|PDB= 1suc |SIZE=350|CAPTION= <scene name='initialview01'>1suc</scene>, resolution 1.8Å | |PDB= 1suc |SIZE=350|CAPTION= <scene name='initialview01'>1suc</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=CYA:TWO+OXYGEN+ATOMS+BOUND+TO+SG+OF+CYS'>CYA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1suc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1suc OCA], [http://www.ebi.ac.uk/pdbsum/1suc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1suc RCSB]</span> | |||
}} | }} | ||
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[[Category: Gallagher, T.]] | [[Category: Gallagher, T.]] | ||
[[Category: Gilliland, G L.]] | [[Category: Gilliland, G L.]] | ||
[[Category: hydrolase(serine proteinase)]] | [[Category: hydrolase(serine proteinase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:47:08 2008'' | ||
Revision as of 23:47, 30 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Subtilisin, with EC number 3.4.21.62 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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