1KRX

SOLUTION STRUCTURE OF BERYLLOFLUORIDE-ACTIVATED NTRC RECEIVER DOMAIN: MODEL STRUCTURES INCORPORATING ACTIVE SITE CONTACTS

Summary for 1KRX

• Entry DOI: 10.2210/pdb1krx/pdb
• Related: 1DC7 1DC8 1DJM 1F4V 1J56 1KRW
• NMR Information: BMRB: 5303
• Descriptor: NITROGEN REGULATION PROTEIN NR(I), BERYLLIUM TRIFLUORIDE ION (2 entities in total)
• Functional Keywords: two component signal transduction, receiver domain, bef3, phosphorylation, bacterial nitrogen regulatory protein, signaling protein
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 1
• Total formula weight: 13702.61

Authors

Hastings, C.A.,Lee, S.-Y.,Cho, H.S.,Yan, D.,Kustu, S.,Wemmer, D.E. (deposition date: 2002-01-10, release date: 2003-08-19, Last modification date: 2024-05-22)

Primary citation

Hastings, C.A.,Lee, S.-Y.,Cho, H.S.,Yan, D.,Kustu, S.,Wemmer, D.E.
High-Resolution Solution Structure of the Beryllofluoride-Activated NtrC Receiver Domain
Biochemistry, 42:9081-9090, 2003

PubMed Abstract: Bacterial receiver domains mediate the cellular response to environmental changes through conformational changes induced by phosphorylation of a conserved aspartate residue. While the structures of several activated receiver domains have recently been determined, there is substantial variation in the conformational changes occurring upon activation. Here we present the high-resolution structure of the activated NtrC receiver domain (BeF(3)(-)-NtrC(r) complex) determined using NMR data, including residual dipolar couplings, yielding a family of structures with a backbone rmsd of 0.57 +/- 0.08 A, which is compared with the previous lower-resolution structure of the phosphorylated protein. Both phosphorylation and beryllofluoride addition induce a shift in register and an axial rotation of alpha-helix 4. In this high-resolution structure, we are able to observe a concerted change in the positions of Thr82 and Tyr101; this correlated change in two conserved residues (termed Y-T coupling) has been considered a general feature of the conformational change in receiver domains upon activation. In NtrC, this correlated side chain shift, leading to the helix reorientation, is distinctly different from the smaller reorganization seen in other activated receiver domains, and involves numerous other residues which do not participate in conformational changes seen in the other systems. Titration of the activated receiver domain with peptides from the NtrC ATPase domain provides direct evidence for interactions on the rearranged face of the receiver domain, which are likely to be responsible for enabling assembly into the active aggregate. Analysis of the active structure also suggests that His84 may play a role in controlling the phosphate hydrolysis rate.

PubMed: 12885241
DOI: 10.1021/bi0273866

Experimental method

SOLUTION NMR