1vsb: Difference between revisions
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[[Image:1vsb.gif|left|200px]]<br /><applet load="1vsb" size=" | [[Image:1vsb.gif|left|200px]]<br /><applet load="1vsb" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1vsb, resolution 2.1Å" /> | caption="1vsb, resolution 2.1Å" /> | ||
'''SUBTILISIN CARLSBERG L-PARA-CHLOROPHENYL-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX'''<br /> | '''SUBTILISIN CARLSBERG L-PARA-CHLOROPHENYL-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1VSB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. 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] Known structural/functional Sites: <scene name='pdbsite=ACT:SER Of Active Site Has Been Chemically Modified To Inclu ...'>ACT</scene>, <scene name='pdbsite=M1:Ca Metal Binding Site 1'>M1</scene> and <scene name='pdbsite=M2:Ca Metal Binding Site 2'>M2</scene>. Full crystallographic information is available from [http:// | 1VSB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. 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] Known structural/functional Sites: <scene name='pdbsite=ACT:SER+Of+Active+Site+Has+Been+Chemically+Modified+To+Inclu+...'>ACT</scene>, <scene name='pdbsite=M1:Ca+Metal+Binding+Site+1'>M1</scene> and <scene name='pdbsite=M2:Ca+Metal+Binding+Site+2'>M2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VSB OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
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Revision as of 11:17, 3 February 2008
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SUBTILISIN CARLSBERG L-PARA-CHLOROPHENYL-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX
OverviewOverview
In order to probe the structural basis of stereoselectivity in the serine, protease family, a series of enantiomeric boronic acids, RCH2CH(NHCOCH3)B(OH)2 has been synthesized and kinetically characterized, as transition-state analog inhibitors using alpha-chymotrypsin and, subtilisin Carlsberg as model systems. When the R-substituent in this, series was changed from a p-chlorophenyl to a 1-naphthyl group, alpha-chymotrypsin, but not subtilisin, reversed its usual preference for, l-enantiomers and bound more tightly to the D-enantiomer [Martichonok, V., & Jones, J. B. (1996) J. Am. Chem. Soc. 118, 950-958]. The structural, factors responsible for the differences in stereoselectivity between the, two enzymes have been explored by X-ray crystallographic examination of, subtilisin Carlsberg and gamma-chymotrypsin complexes of the L- and, D-enantiomers of p-chlorophenyl and 1-naphthyl boronic acid derivatives., In both enzymes, the L-isomers of the inhibitors, which are more closely, related to the natural L-amino acid substrates, form tetrahedral adducts, covalently linking the central boron atom and Ogamma of the catalytic, serine. The d-isomers, however, differ in the way they interact with, subtilisin or gamma-chymotrypsin. With subtilisin, both the, D-p-chlorophenyl and D-1-naphthyl inhibitor complexes form covalent Ser, Ogamma-to-boron bonds, but with gamma-chymotrypsin, the same inhibitors, lead to novel tetrahedral adducts covalently linking both Ser195 Ogamma, and His57 Nepsilon2 covalently via the boron atom.
About this StructureAbout this Structure
1VSB is a Single protein structure of sequence from Bacillus licheniformis. Active as Subtilisin, with EC number 3.4.21.62 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
ReferenceReference
Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes., Stoll VS, Eger BT, Hynes RC, Martichonok V, Jones JB, Pai EF, Biochemistry. 1998 Jan 13;37(2):451-62. PMID:9425066
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