4HYE

Crystal structure of a response regulator spr1814 from Streptococcus pneumoniae reveals unique interdomain contacts among NarL family proteins

Summary for 4HYE

• Entry DOI: 10.2210/pdb4hye/pdb
• Descriptor: Response regulator (2 entities in total)
• Functional Keywords: cytosol, transcription activator
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 2
• Total formula weight: 49198.44

Authors

Park, A.K.,Moon, J.H.,Chi, Y.M. (deposition date: 2012-11-13, release date: 2013-06-05, Last modification date: 2024-03-20)

Primary citation

Park, A.K.,Moon, J.H.,Oh, J.S.,Lee, K.S.,Chi, Y.M.
Crystal structure of the response regulator spr1814 from Streptococcus pneumoniae reveals unique interdomain contacts among NarL family proteins.
Biochem.Biophys.Res.Commun., 434:65-69, 2013

PubMed Abstract: Spr1814 belongs to the NarL/FixJ subfamily of signal transduction response regulators (RR), and has been predicted to regulate the neighboring ABC transporter, which translocates antibiotic molecules in Streptococcus pneumoniae. Here, we report the crystal structure of full-length unphosphorylated spr1814 at 1.7Å resolution. The asymmetric unit contains two spr1814 molecules, which display very different conformations. Through comparisons with other RRs structures, we concluded that one molecule adopts a general inactive conformation, whereas the other molecule adopts an intermediate conformation. The superposition of each molecule showed that rotational change of the effector domain occurred in intermediate conformational state, implying that domain rearrangement could occur upon phosphorylation.

PubMed: 23545256
DOI: 10.1016/j.bbrc.2013.03.065

Experimental method

X-RAY DIFFRACTION (1.7 Å)