1be6
From Proteopedia
(New page: 200px<br /> <applet load="1be6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1be6, resolution 2.15Å" /> '''TRANS-CINNAMOYL-SUB...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1BE6 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 CA, TCA and CCN as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BE6 OCA]]. | + | 1BE6 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 CA, TCA and CCN as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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 Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BE6 OCA]]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Bacillus licheniformis]] | [[Category: Bacillus licheniformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Subtilisin]] | ||
[[Category: Klibanov, A.M.]] | [[Category: Klibanov, A.M.]] | ||
[[Category: Schmitke, J.L.]] | [[Category: Schmitke, J.L.]] | ||
| Line 24: | Line 25: | ||
[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:42:40 2007'' |
Revision as of 11:37, 30 October 2007
|
TRANS-CINNAMOYL-SUBTILISIN IN ANHYDROUS ACETONITRILE
Overview
The x-ray crystal structures of trans-cinnamoyl-subtilisin, an acyl-enzyme, covalent intermediate of the serine protease subtilisin Carlsberg, have, been determined to 2.2-A resolution in anhydrous acetonitrile and in, water. The cinnamoyl-subtilisin structures are virtually identical in the, two solvents. In addition, their enzyme portions are nearly, indistinguishable from previously determined structures of the free enzyme, in acetonitrile and in water; thus, acylation in either aqueous or, nonaqueous solvent causes no appreciable conformational changes. However, the locations of bound solvent molecules in the active site of the acyl-, and free enzyme forms in acetonitrile and in water are distinct. Such, differences in the active site solvation may contribute to the observed, ... [(full description)]
About this Structure
1BE6 is a [Single protein] structure of sequence from [Bacillus licheniformis] with CA, TCA and CCN as [ligands]. Active as [Subtilisin], with EC number [3.4.21.62]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
Reference
Comparison of x-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water., Schmitke JL, Stern LJ, Klibanov AM, Proc Natl Acad Sci U S A. 1998 Oct 27;95(22):12918-23. PMID:9789015
Page seeded by OCA on Tue Oct 30 13:42:40 2007
