1xvm

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[[Image:1xvm.gif|left|200px]]
[[Image:1xvm.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1xvm |SIZE=350|CAPTION= <scene name='initialview01'>1xvm</scene>, resolution 1.10&Aring;
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The line below this paragraph, containing "STRUCTURE_1xvm", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE=
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{{STRUCTURE_1xvm| PDB=1xvm | SCENE= }}
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|RELATEDENTRY=[[1xvo|1XVO]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xvm OCA], [http://www.ebi.ac.uk/pdbsum/1xvm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xvm RCSB]</span>
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}}
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'''Trypsin from Fusarium oxysporum- room temperature to atomic resolution'''
'''Trypsin from Fusarium oxysporum- room temperature to atomic resolution'''
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[[Category: Lamzin, V S.]]
[[Category: Lamzin, V S.]]
[[Category: Schmidt, A.]]
[[Category: Schmidt, A.]]
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[[Category: atomic resolution]]
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[[Category: Atomic resolution]]
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[[Category: mobility]]
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[[Category: Mobility]]
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[[Category: room temperature]]
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[[Category: Room temperature]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:33:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:55:16 2008''
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Revision as of 12:33, 3 May 2008

Image:1xvm.gif

Template:STRUCTURE 1xvm

Trypsin from Fusarium oxysporum- room temperature to atomic resolution


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.

About this Structure

1XVM is a Single protein structure of sequence from Fusarium oxysporum. Full crystallographic information is available from OCA.

Reference

Extraction of functional motion in trypsin crystal structures., Schmidt A, Lamzin VS, Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1132-9. Epub 2005, Jul 20. PMID:16041079 Page seeded by OCA on Sat May 3 15:33:48 2008

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