From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1xj2.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1xj2.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1xj2| PDB=1xj2 | SCENE= }} | | {{STRUCTURE_1xj2| PDB=1xj2 | SCENE= }} |
| | | | |
| - | '''CO-bound structure of bjFixLH'''
| + | ===CO-bound structure of bjFixLH=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Rhizobia directly regulate the expression of genes required for symbiotic nitrogen fixation in response to oxygen concentration via the sensor protein FixL. The N-terminal PAS domain of FixL contains a histidine-coordinated heme and regulates the activity of its effector domain, a C-terminal histidine kinase, in response to binding of oxygen and other ligands at the heme. To further investigate ligand-induced inhibition of FixL, we have determined the crystal structures of the heme domain in both the deoxy state and bound to carbon monoxide, a weak inhibitor of FixL kinase activity. Structures collected at room temperature are presented in each state from two crystallographic space groups at 1.8 and 2 A resolution. These structures reveal displacement of the residues of the H(beta) and I(beta) strands by Leu236 upon CO binding, and this structural change propagates more than 15 A to a region of the structure implicated in signal transduction in PAS proteins. Displacement of residues Ile215, Ile216, and Gly217 in the FG loop is also evident, accompanied by the movement of heme propionate 6 upon change in iron ligation. CO binding increases the temperature factors in the FG loop of the protein and disorders the side chain of Arg206, a conserved residue involved in the FG loop switch mechanism. We relate these results to structural changes in other PAS sensor domains and their involvement in catalytic control.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15779889}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15779889 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_15779889}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| | [[Category: Oxygen sensor]] | | [[Category: Oxygen sensor]] |
| | [[Category: Pas domain]] | | [[Category: Pas domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:05:39 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:00:24 2008'' |
Revision as of 16:00, 27 July 2008
Template:STRUCTURE 1xj2
CO-bound structure of bjFixLH
Template:ABSTRACT PUBMED 15779889
About this Structure
1XJ2 is a Single protein structure of sequence from Bradyrhizobium japonicum. Full crystallographic information is available from OCA.
Reference
Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling., Key J, Moffat K, Biochemistry. 2005 Mar 29;44(12):4627-35. PMID:15779889
Page seeded by OCA on Sun Jul 27 19:00:24 2008
