1scb: Difference between revisions

Revision as of 23:05, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1scb.png

Template:STRUCTURE 1scb

ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENTENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT

Template:ABSTRACT PUBMED 8378343

About this StructureAbout this Structure

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

ReferenceReference

Enzyme crystal structure in a neat organic solvent., Fitzpatrick PA, Steinmetz AC, Ringe D, Klibanov AM, Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8653-7. PMID:8378343

Page seeded by OCA on Sun Jul 27 23:05:15 2008

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OCA

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-'''ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT'''
+===ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT===
-==Overview==
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-The crystal structure of the serine protease subtilisin Carlsberg in anhydrous acetonitrile was determined at 2.3 A resolution. It was found to be essentially identical to the three-dimensional structure of the enzyme in water; the differences observed were smaller than those between two independently determined structures in aqueous solution. The hydrogen bond system of the catalytic triad is intact in acetonitrile. The majority (99 of 119) of enzyme-bound, structural water molecules have such a great affinity to subtilisin that they are not displaced even in anhydrous acetonitrile. Of the 12 enzyme-bound acetonitrile molecules, 4 displace water molecules and 8 bind where no water had been observed before. One-third of all subtilisin-bound acetonitrile molecules reside in the active center, occupying the same region (P1, P2, and P3 binding sites) as the specific protein inhibitor eglin c.
+The line below this paragraph, {{ABSTRACT_PUBMED_8378343}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_8378343}}
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 [[Category: Steinmetz, A C.U.]]
 [[Category: Serine protease]]
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