1gns

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[[Image:1gns.jpg|left|200px]]<br /><applet load="1gns" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gns.jpg|left|200px]]
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caption="1gns, resolution 1.8&Aring;" />
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'''SUBTILISIN BPN''''<br />
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{{Structure
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|PDB= 1gns |SIZE=350|CAPTION= <scene name='initialview01'>1gns</scene>, resolution 1.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACN:ACETONE'>ACN</scene>
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|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]
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|GENE=
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}}
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'''SUBTILISIN BPN''''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1GNS 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=ACN:'>ACN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1GNS OCA].
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1GNS 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=1GNS OCA].
==Reference==
==Reference==
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Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'., Almog O, Gallagher DT, Ladner JE, Strausberg S, Alexander P, Bryan P, Gilliland GL, J Biol Chem. 2002 Jul 26;277(30):27553-8. Epub 2002 May 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12011071 12011071]
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Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'., Almog O, Gallagher DT, Ladner JE, Strausberg S, Alexander P, Bryan P, Gilliland GL, J Biol Chem. 2002 Jul 26;277(30):27553-8. Epub 2002 May 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12011071 12011071]
[[Category: Bacillus amyloliquefaciens]]
[[Category: Bacillus amyloliquefaciens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: serine proteinase]]
[[Category: serine proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:25:33 2008''

Revision as of 09:25, 20 March 2008


PDB ID 1gns

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands:
Activity: Subtilisin, with EC number 3.4.21.62
Coordinates: save as pdb, mmCIF, xml



SUBTILISIN BPN'


Overview

The crystal structures of two thermally stabilized subtilisin BPN' variants, S63 and S88, are reported here at 1.8 and 1.9 A resolution, respectively. The micromolar affinity calcium binding site (site A) has been deleted (Delta75-83) in these variants, enabling the activity and thermostability measurements in chelating conditions. Each of the variants includes mutations known previously to increase the thermostability of calcium-independent subtilisin in addition to new stabilizing mutations. S63 has eight amino acid replacements: D41A, M50F, A73L, Q206W, Y217K, N218S, S221C, and Q271E. S63 has 75-fold greater stability than wild type subtilisin in chelating conditions (10 mm EDTA). The other variant, S88, has ten site-specific changes: Q2K, S3C, P5S, K43N, M50F, A73L, Q206C, Y217K, N218S, and Q271E. The two new cysteines form a disulfide bond, and S88 has 1000 times greater stability than wild type subtilisin in chelating conditions. Comparisons of the two new crystal structures (S63 in space group P2(1) with A cell constants 41.2, 78.1, 36.7, and beta = 114.6 degrees and S88 in space group P2(1)2(1)2(1) with cell constants 54.2, 60.4, and 82.7) with previous structures of subtilisin BPN' reveal that the principal changes are in the N-terminal region. The structural bases of the stabilization effects of the new mutations Q2K, S3C, P5S, D41A, Q206C, and Q206W are generally apparent. The effects are attributed to the new disulfide cross-link and to improved hydrophobic packing, new hydrogen bonds, and other rearrangements in the N-terminal region.

About this Structure

1GNS is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.

Reference

Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'., Almog O, Gallagher DT, Ladner JE, Strausberg S, Alexander P, Bryan P, Gilliland GL, J Biol Chem. 2002 Jul 26;277(30):27553-8. Epub 2002 May 13. PMID:12011071

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