1av7
From Proteopedia
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| - | [[Image:1av7.gif|left|200px]] | + | [[Image:1av7.gif|left|200px]] |
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| - | '''SUBTILISIN CARLSBERG L-NAPHTHYL-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX''' | + | {{Structure |
| + | |PDB= 1av7 |SIZE=350|CAPTION= <scene name='initialview01'>1av7</scene>, resolution 2.6Å | ||
| + | |SITE= <scene name='pdbsite=ACT:SER+Of+Active+Site+Has+Been+Chemically+Modified+To+Inclu+...'>ACT</scene>, <scene name='pdbsite=M1:Na+Metal+Binding+Site+1'>M1</scene> and <scene name='pdbsite=M2:Na+Metal+Binding+Site+2'>M2</scene> | ||
| + | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SUBTILISIN CARLSBERG L-NAPHTHYL-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AV7 is a [ | + | 1AV7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AV7 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9425066 9425066] |
[[Category: Bacillus licheniformis]] | [[Category: Bacillus licheniformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Stoll, V S.]] | [[Category: Stoll, V S.]] | ||
[[Category: NA]] | [[Category: NA]] | ||
| - | [[Category: boronic acid | + | [[Category: boronic acid inhibitor]] |
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:41 2008'' |
Revision as of 08:02, 20 March 2008
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| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | |||||||
| Activity: | Subtilisin, with EC number 3.4.21.62 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SUBTILISIN CARLSBERG L-NAPHTHYL-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX
Overview
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 Structure
1AV7 is a Single protein structure of sequence from Bacillus licheniformis. Full crystallographic information is available from OCA.
Reference
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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