1xvo: Difference between revisions

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New page: left|200px<br /><applet load="1xvo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xvo, resolution 0.84Å" /> '''Trypsin from Fusariu...
 
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[[Image:1xvo.gif|left|200px]]<br /><applet load="1xvo" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1xvo.gif|left|200px]]<br /><applet load="1xvo" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1xvo, resolution 0.84&Aring;" />
caption="1xvo, resolution 0.84&Aring;" />
'''Trypsin from Fusarium oxysporum at pH 6'''<br />
'''Trypsin from Fusarium oxysporum at pH 6'''<br />


==Overview==
==Overview==
The analysis of anisotropic atomic displacement parameters for the direct, extraction of functionally relevant motion from X-ray crystal structures, of Fusarium oxysporum trypsin is presented. Several atomic resolution, structures complexed with inhibitors or substrates and determined at, different pH values and temperatures were investigated. The analysis, revealed a breathing-like molecular motion conserved across trypsin, structures from two organisms and three different crystal forms., Directional motion was observed suggesting a change of the width of the, substrate-binding cleft and a change in the length of the specificity, pocket. The differences in direction of motion across the structures are, dependent on the mode of substrate or inhibitor binding and the chemical, environment around the active-site residues. Together with the occurrence, of multiple-residue conformers, they reflect spatial rearrangement, throughout the deacylation pathway.
The analysis of anisotropic atomic displacement parameters for the direct extraction of functionally relevant motion from X-ray crystal structures of Fusarium oxysporum trypsin is presented. Several atomic resolution structures complexed with inhibitors or substrates and determined at different pH values and temperatures were investigated. The analysis revealed a breathing-like molecular motion conserved across trypsin structures from two organisms and three different crystal forms. Directional motion was observed suggesting a change of the width of the substrate-binding cleft and a change in the length of the specificity pocket. The differences in direction of motion across the structures are dependent on the mode of substrate or inhibitor binding and the chemical environment around the active-site residues. Together with the occurrence of multiple-residue conformers, they reflect spatial rearrangement throughout the deacylation pathway.


==About this Structure==
==About this Structure==
1XVO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XVO OCA].  
1XVO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XVO OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Trypsin]]
[[Category: Trypsin]]
[[Category: Lamzin, V.S.]]
[[Category: Lamzin, V S.]]
[[Category: Schmidt, A.]]
[[Category: Schmidt, A.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: trypsin]]
[[Category: trypsin]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:22:37 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:59:08 2008''