3bnc
From Proteopedia
(New page: 200px {{Structure |PDB= 3bnc |SIZE=350|CAPTION= <scene name='initialview01'>3bnc</scene>, resolution 1.65Å |SITE= <scene name='pdbsite=AC1:Fe+Binding+Site+F...) |
|||
Line 1: | Line 1: | ||
[[Image:3bnc.jpg|left|200px]] | [[Image:3bnc.jpg|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_3bnc", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | + | {{STRUCTURE_3bnc| PDB=3bnc | SCENE= }} | |
- | | | + | |
- | + | ||
- | }} | + | |
'''Lipoxygenase-1 (Soybean) I553G Mutant''' | '''Lipoxygenase-1 (Soybean) I553G Mutant''' | ||
Line 27: | Line 24: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Tomchick, D R.]] | [[Category: Tomchick, D R.]] | ||
- | [[Category: | + | [[Category: Cytoplasm]] |
- | [[Category: | + | [[Category: Dioxygenase]] |
- | [[Category: | + | [[Category: Fatty acid biosynthesis]] |
- | [[Category: | + | [[Category: Fatty acid]] |
- | [[Category: | + | [[Category: Iron]] |
- | [[Category: | + | [[Category: Lipid synthesis]] |
- | [[Category: | + | [[Category: Lipoxygenase]] |
- | [[Category: | + | [[Category: Metal-binding]] |
- | [[Category: | + | [[Category: Metalloprotein]] |
- | [[Category: | + | [[Category: Oxidoreductase]] |
- | [[Category: | + | [[Category: Oxylipin biosynthesis]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:55:53 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 17:55, 4 May 2008
Lipoxygenase-1 (Soybean) I553G Mutant
Overview
This study examines the impact of a series of mutations at position 553 on the kinetic and structural properties of soybean lipoxygenase-1 (SLO-1). The previously uncharacterized mutants reported herein are I553L, I553V, and I553G. High-resolution x-ray studies of these mutants, together with the earlier studied I553A, show almost no structural change in relation to the WT-enzyme. By contrast, a progression in kinetic behavior occurs in which the decrease in the size of the side chain at position 553 leads to an increased importance of donor-acceptor distance sampling in the course of the hydrogen transfer process. These dynamical changes in behavior are interpreted in the context of two general classes of protein motions, preorganization and reorganization, with the latter including the distance sampling modes [Klinman JP (2006) Philos Trans R Soc London Ser B 361:1323-1331; Nagel Z, Klinman JP (2006) Chem Rev 106:3095-3118]. The aggregate data for SLO-1 show how judicious placement of hydrophobic side chains can influence enzyme catalysis via enhanced donor-acceptor hydrogenic wave function overlap.
About this Structure
3BNC is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
Reference
Enzyme structure and dynamics affect hydrogen tunneling: the impact of a remote side chain (I553) in soybean lipoxygenase-1., Meyer MP, Tomchick DR, Klinman JP, Proc Natl Acad Sci U S A. 2008 Jan 29;105(4):1146-51. Epub 2008 Jan 23. PMID:18216254 Page seeded by OCA on Sun May 4 20:55:53 2008