1be6
From Proteopedia
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| - | [[Image:1be6.gif|left|200px]] | + | [[Image:1be6.gif|left|200px]] |
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| - | '''TRANS-CINNAMOYL-SUBTILISIN IN ANHYDROUS ACETONITRILE''' | + | {{Structure |
| + | |PDB= 1be6 |SIZE=350|CAPTION= <scene name='initialview01'>1be6</scene>, resolution 2.15Å | ||
| + | |SITE= <scene name='pdbsite=ACT:Active+Site'>ACT</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TCA:PHENYLETHYLENECARBOXYLIC+ACID'>TCA</scene> and <scene name='pdbligand=CCN:ACETONITRILE'>CCN</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= | ||
| + | }} | ||
| + | |||
| + | '''TRANS-CINNAMOYL-SUBTILISIN IN ANHYDROUS ACETONITRILE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BE6 is a [ | + | 1BE6 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=1BE6 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9789015 9789015] |
[[Category: Bacillus licheniformis]] | [[Category: Bacillus licheniformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[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 10:09:49 2008'' |
Revision as of 08:09, 20 March 2008
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| , resolution 2.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , and | ||||||
| Activity: | Subtilisin, with EC number 3.4.21.62 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 variations in enzymatic activities. On prolonged exposure to organic solvent or removal of interstitial solvent from the crystal lattice, the channels within enzyme crystals are shown to collapse, leading to a drop in the number of active sites accessible to the substrate. The mechanistic and preparative implications of our findings for enzymatic catalysis in organic solvents are discussed.
About this Structure
1BE6 is a Single protein structure of sequence from Bacillus licheniformis. 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
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