1rnl
From Proteopedia
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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 ... [(full description)]
About this Structure
1RNL is a [Single protein] structure of sequence from [Escherichia coli] with PT and GOL as [ligands]. 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
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