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1av7

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==About this Structure==
==About this Structure==
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1AV7 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]] with NA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Hydrolase Hydrolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62]]. Structure known Active Sites: ACT, M1 and M2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AV7 OCA]].
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1AV7 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]] with NA 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]]. Structure known Active Sites: ACT, M1 and M2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AV7 OCA]].
==Reference==
==Reference==
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[[Category: Bacillus licheniformis]]
[[Category: Bacillus licheniformis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Subtilisin]]
[[Category: Eger, B.T.]]
[[Category: Eger, B.T.]]
[[Category: Hynes, R.C.]]
[[Category: Hynes, R.C.]]
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[[Category: serine protease]]
[[Category: serine protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:43:47 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:42:44 2007''

Revision as of 08:38, 30 October 2007


1av7, resolution 2.6Å

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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 ... [(full description)]

About this Structure

1AV7 is a [Single protein] structure of sequence from [Bacillus licheniformis] with NA as [ligand]. Active as [Subtilisin], with EC number [3.4.21.62]. Structure known Active Sites: ACT, M1 and M2. 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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