From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1rnl.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1rnl.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1rnl| PDB=1rnl | SCENE= }} | | {{STRUCTURE_1rnl| PDB=1rnl | SCENE= }} |
| | | | |
| - | '''THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL FROM NARL'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8780507}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8780507 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_8780507}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 31: |
Line 35: |
| | [[Category: Signal transduction protein]] | | [[Category: Signal transduction protein]] |
| | [[Category: Two-component system]] | | [[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 Mon Jul 28 12:21:38 2008'' |
Revision as of 09:21, 28 July 2008
Template:STRUCTURE 1rnl
THE NITRATE/NITRITE RESPONSE REGULATOR PROTEIN NARL FROM NARL
Template:ABSTRACT PUBMED 8780507
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 Mon Jul 28 12:21:38 2008
