1rnl
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1rnl.jpg|left|200px]] | [[Image:1rnl.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1rnl", 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_1rnl| PDB=1rnl | SCENE= }} |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL FROM NARL''' | '''THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL FROM NARL''' | ||
| Line 31: | Line 28: | ||
[[Category: Kaczor-Grzeskowiak, M.]] | [[Category: Kaczor-Grzeskowiak, M.]] | ||
[[Category: Schroder, I.]] | [[Category: Schroder, I.]] | ||
| - | [[Category: | + | [[Category: Response regulator]] |
| - | [[Category: | + | [[Category: Signal transduction protein]] |
| - | [[Category: | + | [[Category: Two-component system]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:42:14 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 04:42, 3 May 2008
THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL FROM NARL
Overview
The crystal structure analysis of the NarL protein provides a first look at interactions between receiver and effector domains of a full-length bacterial response regulator. The N-terminal receiver domain, with 131 amino acids, is folded into a 5-strand beta sheet flanked by 5 alpha helices, as seen in CheY and in the N-terminal domain of NTRC. The C-terminal DNA-binding domain, with 62 amino acids, is a compact bundle of 4 alpha helices, of which the middle 2 form a helix-turn-helix motif closely related to that of Drosophila paired protein and other H-T-H DNA-binding proteins. The 2 domains are connected by an alpha helix of 10 amino acids and a 13-residue flexible tether that is not visible and presumably disordered in the X-ray structure. In this unphosphorylated form of NarL, the C-terminal domain is turned against the receiver domain in a manner that would preclude DNA binding. Activation of NarL via phosphorylation of Asp59 must involve transfer of information to the interdomain interface and either rotation or displacement of the DNA-binding C-terminal domain. Docking of a B-DNA duplex against the isolated C-terminal domain in the manner observed in paired protein and other H-T-H proteins suggests a stereochemical basis for DNA sequence preference: T-R-C-C-Y (high affinity) or T-R-C-T-N (low affinity), which is close to the experimentally observed consensus sequence: T-A-C-Y-N. The NarL structure is a model for other members of the FixJ or LuxR family of bacterial transcriptional activators, and possibly to the more distant OmpR and NtrC families as well.
About this Structure
1RNL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of the Escherichia coli response regulator NarL., Baikalov I, Schroder I, Kaczor-Grzeskowiak M, Grzeskowiak K, Gunsalus RP, Dickerson RE, Biochemistry. 1996 Aug 27;35(34):11053-61. PMID:8780507 Page seeded by OCA on Sat May 3 07:42:14 2008
