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1sub

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[[Image:1sub.jpg|left|200px]]
[[Image:1sub.jpg|left|200px]]
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{{Structure
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|PDB= 1sub |SIZE=350|CAPTION= <scene name='initialview01'>1sub</scene>, resolution 1.75&Aring;
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The line below this paragraph, containing "STRUCTURE_1sub", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CYA:TWO+OXYGEN+ATOMS+BOUND+TO+SG+OF+CYS'>CYA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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{{STRUCTURE_1sub| PDB=1sub | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sub OCA], [http://www.ebi.ac.uk/pdbsum/1sub PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sub RCSB]</span>
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'''CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN'''
'''CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN'''
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[[Category: Gallagher, T.]]
[[Category: Gallagher, T.]]
[[Category: Gilliland, G L.]]
[[Category: Gilliland, G L.]]
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[[Category: hydrolase(serine proteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:08:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:47:05 2008''
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Revision as of 06:08, 3 May 2008

Image:1sub.jpg

Template:STRUCTURE 1sub

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

1SUB is a Single protein structure of sequence from Bacillus amyloliquefaciens. 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 Page seeded by OCA on Sat May 3 09:08:39 2008

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