1scd

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(New page: 200px<br /><applet load="1scd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1scd, resolution 2.3&Aring;" /> '''X-RAY CRYSTAL STRUCTU...)
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[[Image:1scd.gif|left|200px]]<br /><applet load="1scd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1scd, resolution 2.3&Aring;" />
caption="1scd, resolution 2.3&Aring;" />
'''X-RAY CRYSTAL STRUCTURE OF CROSS-LINKED SUBTILISM CARLSBERG IN WATER VS. ACETONITRILE'''<br />
'''X-RAY CRYSTAL STRUCTURE OF CROSS-LINKED SUBTILISM CARLSBERG IN WATER VS. ACETONITRILE'''<br />
==Overview==
==Overview==
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The crystal structure of subtilisin Carlsberg lightly cross-linked with, glutaraldehyde was solved in aqueous solution by X-ray crystallography at, 2.3 A resolution. It was found to be virtually identical to the recently, determined (Fitzpatrick, P.A., Steinmetz, A.C.U., Ringe, D.A. &amp; Klibanov, A.M. (1993) Proc. Natl. Acad. Sci. USA 90, 8653) structure of the, cross-linked enzyme in anhydrous acetonitrile. The latter structure was, found to be significantly more rigid than in water, as reflected by their, average B factors. The numbers of subtilisin-bound water molecules in the, two structures are similar (114 and 99 in water and in acetonitrile, respectively), but the locations of some half of these bound waters are, distinct.
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The crystal structure of subtilisin Carlsberg lightly cross-linked with glutaraldehyde was solved in aqueous solution by X-ray crystallography at 2.3 A resolution. It was found to be virtually identical to the recently determined (Fitzpatrick, P.A., Steinmetz, A.C.U., Ringe, D.A. &amp; Klibanov, A.M. (1993) Proc. Natl. Acad. Sci. USA 90, 8653) structure of the cross-linked enzyme in anhydrous acetonitrile. The latter structure was found to be significantly more rigid than in water, as reflected by their average B factors. The numbers of subtilisin-bound water molecules in the two structures are similar (114 and 99 in water and in acetonitrile, respectively), but the locations of some half of these bound waters are distinct.
==About this Structure==
==About this Structure==
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1SCD 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 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SCD OCA].
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1SCD 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 <scene name='pdbligand=CA:'>CA</scene> 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCD OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Subtilisin]]
[[Category: Subtilisin]]
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[[Category: Fitzpatrick, P.A.]]
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[[Category: Fitzpatrick, P A.]]
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[[Category: Klibanov, A.M.]]
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[[Category: Klibanov, A M.]]
[[Category: Ringe, D.]]
[[Category: Ringe, D.]]
[[Category: CA]]
[[Category: CA]]
[[Category: serine protease]]
[[Category: serine protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:16:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:02 2008''

Revision as of 13:00, 21 February 2008


1scd, resolution 2.3Å

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X-RAY CRYSTAL STRUCTURE OF CROSS-LINKED SUBTILISM CARLSBERG IN WATER VS. ACETONITRILE

Overview

The crystal structure of subtilisin Carlsberg lightly cross-linked with glutaraldehyde was solved in aqueous solution by X-ray crystallography at 2.3 A resolution. It was found to be virtually identical to the recently determined (Fitzpatrick, P.A., Steinmetz, A.C.U., Ringe, D.A. & Klibanov, A.M. (1993) Proc. Natl. Acad. Sci. USA 90, 8653) structure of the cross-linked enzyme in anhydrous acetonitrile. The latter structure was found to be significantly more rigid than in water, as reflected by their average B factors. The numbers of subtilisin-bound water molecules in the two structures are similar (114 and 99 in water and in acetonitrile, respectively), but the locations of some half of these bound waters are distinct.

About this Structure

1SCD is a Single protein structure of sequence from Bacillus licheniformis with as ligand. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.

Reference

X-ray crystal structure of cross-linked subtilisin Carlsberg in water vs. acetonitrile., Fitzpatrick PA, Ringe D, Klibanov AM, Biochem Biophys Res Commun. 1994 Jan 28;198(2):675-81. PMID:8297378

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