Crystal structure of receiver domain of putative NarL family response regulator spr1814 from Streptococcus pneumoniae in the absence and presence of the phosphoryl analog beryllofluoride

Ae Kyung Park, Jin Ho Moon, Ki Seog Lee, Young Min Chi

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Spr1814 of Streptococcus pneumoniae is a putative response regulator (RR) that has four-helix helix-turn-helix DNA-binding domain and belongs to the NarL family. The prototypical RR contains two domains, an N-terminal receiver domain linked to a variable effector domain. The receiver domain functions as a phosphorylation-activated switch and contains the typical doubly wound five-stranded α/β fold. Here, we report the crystal structure of the receiver domain of spr1814 (spr1814 R) determined in the absence and presence of beryllofluoride as a phosphoryl analog. Based on the overall structure, spr1814 R was shown to contain the typical fold similar with other structures of the receiver domain; however, an additional linker region connecting the receiver and DNA-binding domain was inserted into the dimer interface of spr1814 R, resulting in the formation of unique dimer interface. Upon phosphorylation, the conformational change of the linker region was observed and this suggests that domain rearrangement between the receiver domain and effector domain could occur in full-length spr1814.

Original languageEnglish
Pages (from-to)403-407
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume421
Issue number2
DOIs
Publication statusPublished - 2012 May 4

Fingerprint

Phosphorylation
Streptococcus pneumoniae
Dimers
Crystal structure
DNA
Switches
Wounds and Injuries
beryllium fluoride

Keywords

  • Phosphoryl analog beryllofluoride
  • Receiver domain
  • Response regulator
  • Two-component phosphotransfer pathways

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

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title = "Crystal structure of receiver domain of putative NarL family response regulator spr1814 from Streptococcus pneumoniae in the absence and presence of the phosphoryl analog beryllofluoride",
abstract = "Spr1814 of Streptococcus pneumoniae is a putative response regulator (RR) that has four-helix helix-turn-helix DNA-binding domain and belongs to the NarL family. The prototypical RR contains two domains, an N-terminal receiver domain linked to a variable effector domain. The receiver domain functions as a phosphorylation-activated switch and contains the typical doubly wound five-stranded α/β fold. Here, we report the crystal structure of the receiver domain of spr1814 (spr1814 R) determined in the absence and presence of beryllofluoride as a phosphoryl analog. Based on the overall structure, spr1814 R was shown to contain the typical fold similar with other structures of the receiver domain; however, an additional linker region connecting the receiver and DNA-binding domain was inserted into the dimer interface of spr1814 R, resulting in the formation of unique dimer interface. Upon phosphorylation, the conformational change of the linker region was observed and this suggests that domain rearrangement between the receiver domain and effector domain could occur in full-length spr1814.",
keywords = "Phosphoryl analog beryllofluoride, Receiver domain, Response regulator, Two-component phosphotransfer pathways",
author = "Park, {Ae Kyung} and Moon, {Jin Ho} and Lee, {Ki Seog} and Chi, {Young Min}",
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T1 - Crystal structure of receiver domain of putative NarL family response regulator spr1814 from Streptococcus pneumoniae in the absence and presence of the phosphoryl analog beryllofluoride

AU - Park, Ae Kyung

AU - Moon, Jin Ho

AU - Lee, Ki Seog

AU - Chi, Young Min

PY - 2012/5/4

Y1 - 2012/5/4

N2 - Spr1814 of Streptococcus pneumoniae is a putative response regulator (RR) that has four-helix helix-turn-helix DNA-binding domain and belongs to the NarL family. The prototypical RR contains two domains, an N-terminal receiver domain linked to a variable effector domain. The receiver domain functions as a phosphorylation-activated switch and contains the typical doubly wound five-stranded α/β fold. Here, we report the crystal structure of the receiver domain of spr1814 (spr1814 R) determined in the absence and presence of beryllofluoride as a phosphoryl analog. Based on the overall structure, spr1814 R was shown to contain the typical fold similar with other structures of the receiver domain; however, an additional linker region connecting the receiver and DNA-binding domain was inserted into the dimer interface of spr1814 R, resulting in the formation of unique dimer interface. Upon phosphorylation, the conformational change of the linker region was observed and this suggests that domain rearrangement between the receiver domain and effector domain could occur in full-length spr1814.

AB - Spr1814 of Streptococcus pneumoniae is a putative response regulator (RR) that has four-helix helix-turn-helix DNA-binding domain and belongs to the NarL family. The prototypical RR contains two domains, an N-terminal receiver domain linked to a variable effector domain. The receiver domain functions as a phosphorylation-activated switch and contains the typical doubly wound five-stranded α/β fold. Here, we report the crystal structure of the receiver domain of spr1814 (spr1814 R) determined in the absence and presence of beryllofluoride as a phosphoryl analog. Based on the overall structure, spr1814 R was shown to contain the typical fold similar with other structures of the receiver domain; however, an additional linker region connecting the receiver and DNA-binding domain was inserted into the dimer interface of spr1814 R, resulting in the formation of unique dimer interface. Upon phosphorylation, the conformational change of the linker region was observed and this suggests that domain rearrangement between the receiver domain and effector domain could occur in full-length spr1814.

KW - Phosphoryl analog beryllofluoride

KW - Receiver domain

KW - Response regulator

KW - Two-component phosphotransfer pathways

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