1c3l

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(New page: 200px<br /><applet load="1c3l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c3l, resolution 2.16&Aring;" /> '''SUBTILISIN-CARLSBERG...)
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[[Image:1c3l.gif|left|200px]]<br /><applet load="1c3l" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1c3l, resolution 2.16&Aring;" />
caption="1c3l, resolution 2.16&Aring;" />
'''SUBTILISIN-CARLSBERG COMPLEXED WITH XENON (8 BAR)'''<br />
'''SUBTILISIN-CARLSBERG COMPLEXED WITH XENON (8 BAR)'''<br />
==Overview==
==Overview==
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X-ray diffraction is used to study the binding of xenon and krypton to a, variety of crystallised proteins: porcine pancreatic elastase; subtilisin, Carlsberg from Bacillus licheniformis; cutinase from Fusarium solani;, collagenase from Hypoderma lineatum; hen egg lysozyme, the lipoamide, dehydrogenase domain from the outer membrane protein P64k from Neisseria, meningitidis; urate-oxidase from Aspergillus flavus, mosquitocidal, delta-endotoxin CytB from Bacillus thuringiensis and the ligand-binding, domain of the human nuclear retinoid-X receptor RXR-alpha. Under gas, pressures ranging from 8 to 20 bar, xenon is able to bind to discrete, sites in hydrophobic cavities, ligand and substrate binding pockets, and, into the pore of channel-like structures. These xenon complexes can be, used to map hydrophobic sites in proteins, or as heavy-atom derivatives in, the isomorphous replacement method of structure determination.
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X-ray diffraction is used to study the binding of xenon and krypton to a variety of crystallised proteins: porcine pancreatic elastase; subtilisin Carlsberg from Bacillus licheniformis; cutinase from Fusarium solani; collagenase from Hypoderma lineatum; hen egg lysozyme, the lipoamide dehydrogenase domain from the outer membrane protein P64k from Neisseria meningitidis; urate-oxidase from Aspergillus flavus, mosquitocidal delta-endotoxin CytB from Bacillus thuringiensis and the ligand-binding domain of the human nuclear retinoid-X receptor RXR-alpha. Under gas pressures ranging from 8 to 20 bar, xenon is able to bind to discrete sites in hydrophobic cavities, ligand and substrate binding pockets, and into the pore of channel-like structures. These xenon complexes can be used to map hydrophobic sites in proteins, or as heavy-atom derivatives in the isomorphous replacement method of structure determination.
==About this Structure==
==About this Structure==
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1C3L 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, XE and FMT 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C3L OCA].
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1C3L 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>, <scene name='pdbligand=XE:'>XE</scene> and <scene name='pdbligand=FMT:'>FMT</scene> 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C3L OCA].
==Reference==
==Reference==
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[[Category: Prange, T.]]
[[Category: Prange, T.]]
[[Category: Schiltz, M.]]
[[Category: Schiltz, M.]]
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[[Category: h, N.Colloc.]]
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[[Category: h, N Colloc.]]
[[Category: CA]]
[[Category: CA]]
[[Category: FMT]]
[[Category: FMT]]
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[[Category: xenon]]
[[Category: xenon]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:08:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:02:01 2008''

Revision as of 10:02, 21 February 2008

Image:1c3l.gif

1c3l, resolution 2.16Å

Drag the structure with the mouse to rotate

SUBTILISIN-CARLSBERG COMPLEXED WITH XENON (8 BAR)

Overview

X-ray diffraction is used to study the binding of xenon and krypton to a variety of crystallised proteins: porcine pancreatic elastase; subtilisin Carlsberg from Bacillus licheniformis; cutinase from Fusarium solani; collagenase from Hypoderma lineatum; hen egg lysozyme, the lipoamide dehydrogenase domain from the outer membrane protein P64k from Neisseria meningitidis; urate-oxidase from Aspergillus flavus, mosquitocidal delta-endotoxin CytB from Bacillus thuringiensis and the ligand-binding domain of the human nuclear retinoid-X receptor RXR-alpha. Under gas pressures ranging from 8 to 20 bar, xenon is able to bind to discrete sites in hydrophobic cavities, ligand and substrate binding pockets, and into the pore of channel-like structures. These xenon complexes can be used to map hydrophobic sites in proteins, or as heavy-atom derivatives in the isomorphous replacement method of structure determination.

About this Structure

1C3L is a Single protein structure of sequence from Bacillus licheniformis with , and as ligands. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.

Reference

Exploring hydrophobic sites in proteins with xenon or krypton., Prange T, Schiltz M, Pernot L, Colloc'h N, Longhi S, Bourguet W, Fourme R, Proteins. 1998 Jan;30(1):61-73. PMID:9443341

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