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| | {{STRUCTURE_2owh| PDB=2owh | SCENE= }} | | {{STRUCTURE_2owh| PDB=2owh | SCENE= }} |
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| - | '''Structure of an early-microsecond photolyzed state of CO-bjFixLH'''
| + | ===Structure of an early-microsecond photolyzed state of CO-bjFixLH=== |
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| - | ==Overview==
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| - | The FixL protein of Bradyrhizobium japonicum is a dimeric oxygen sensor responsible for initiating regulation of transcription of genes encoding proteins involved in nitrogen fixation and oxidative stress. It consists of an N-terminal heme-bound PAS domain, denoted bjFixLH, and a C-terminal histidine kinase domain whose enzymatic activity depends on the ligation state of the heme. To investigate the molecular basis for this dependence and the dynamics associated with conversion between ligated and unligated states, we have conducted time-resolved Laue diffraction studies of CO recombination in bjFixLH. Time-dependent difference Fourier maps from 1 micros to 10 ms after photolysis of the heme-CO bond show movement of the side chain of Leu236 and the H and I beta-strands into the ligand binding pocket formerly occupied by CO. Long-range conformational changes are evident in the protein, driven by relaxation of steric interactions between the bound ligand and amino acid side chains and/or changes in heme stereochemistry. These structural changes fully reverse as CO rebinds to the heme. Spectroscopic measurements of CO recombination kinetics in bjFixLH crystals relate the behavior of crystalline bjFixLH to solution and provide a framework for our time-resolved crystallographic experiments. Analysis of the time-dependent difference Fourier maps by singular value decomposition reveals that only one significant singular value accounts for the data. Thus only two structural states are present, the photolyzed and the CO-bound states. The first left singular vector represents the difference in density between these two states and shows features common to difference maps calculated from the static CO and deoxy states. The first right singular vector represents the time course of this difference density and agrees well with the CO recombination kinetics measured spectroscopically. We refine the structure of the photolyzed state present in the early-microsecond time range and find that it does not differ significantly in conformation from static, deoxy bjFixLH. Thus, structural relaxation from CO-bound to deoxy bjFixLH is complete in less than 1 micros. | + | The line below this paragraph, {{ABSTRACT_PUBMED_17385895}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17385895 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17385895}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Oxygen sensor]] | | [[Category: Oxygen sensor]] |
| | [[Category: Pas domain]] | | [[Category: Pas domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:48:23 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:50:04 2008'' |
Revision as of 02:50, 28 July 2008
Template:STRUCTURE 2owh
Structure of an early-microsecond photolyzed state of CO-bjFixLH
Template:ABSTRACT PUBMED 17385895
About this Structure
2OWH is a Single protein structure of sequence from Bradyrhizobium japonicum. Full crystallographic information is available from OCA.
Reference
Time-resolved crystallographic studies of the heme domain of the oxygen sensor FixL: structural dynamics of ligand rebinding and their relation to signal transduction., Key J, Srajer V, Pahl R, Moffat K, Biochemistry. 2007 Apr 24;46(16):4706-15. Epub 2007 Mar 27. PMID:17385895
Page seeded by OCA on Mon Jul 28 05:50:04 2008
