1c1m: Difference between revisions

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New page: left|200px<br /><applet load="1c1m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c1m, resolution 2.20Å" /> '''PORCINE ELASTASE UND...
 
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[[Image:1c1m.jpg|left|200px]]<br /><applet load="1c1m" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1c1m.jpg|left|200px]]<br /><applet load="1c1m" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1c1m, resolution 2.20&Aring;" />
caption="1c1m, resolution 2.20&Aring;" />
'''PORCINE ELASTASE UNDER XENON PRESSURE (8 BAR)'''<br />
'''PORCINE ELASTASE UNDER XENON PRESSURE (8 BAR)'''<br />


==Overview==
==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.
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==
1C1M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with CA, SO4 and XE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C1M OCA].  
1C1M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=XE:'>XE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C1M OCA].  


==Reference==
==Reference==
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[[Category: Bourguet, W.]]
[[Category: Bourguet, W.]]
[[Category: Fourme, R.]]
[[Category: Fourme, R.]]
[[Category: H, N.Colloc.]]
[[Category: H, N Colloc.]]
[[Category: Longhi, S.]]
[[Category: Longhi, S.]]
[[Category: Pernot, L.]]
[[Category: Pernot, L.]]
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[[Category: xenon]]
[[Category: xenon]]


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