TY - JOUR
T1 - Backbone dynamics of an atypical orphan response regulator protein, Helicobacter pylori 1043
AU - Jeong, Ki Woong
AU - Ko, Hyunsook
AU - Lee, Sung Ah
AU - Hong, Eunmi
AU - Ko, Sunggeon
AU - Cho, Hyun Soo
AU - Lee, Weontae
AU - Kim, Yangmee
PY - 2013/2
Y1 - 2013/2
N2 - An atypical orphan response regulator protein, HP1043 (HP-RR) in Helicobacter pylori, is proven to be essential for cell growth and does not require the well known phosphorelay scheme. HP-RR was identified as a symmetric dimer with two functional domains, an N-terminal regulatory domain (HP-RR r) and a C-terminal effector domain (HP-RRe). HP-RR is a new class of response regulator, as a phosphorylation-independent regulator. Previously, we have presented a detailed three-dimensional structure of HP-RR using NMR spectroscopy and X-ray crystallography. In this study, in order to understand the functional importance of flexibilities in HP-RRr and HP-RRe, T1, T2, heteronuclear NOE experiments have been performed and backbone dynamics of HP-RRr and HP-RR e were investigated. HP-RRr is a symmetric dimer and the interface region, α4-β5-α5 of dimer, showed high rigidity (high S 2 values). Site of rearrangements associated with phosphorylation of HP-RRr (Ser75: R ex = 3.382, Ile 95: R ex = 5.228) showed slow chemical exchanges. HP-RRe is composed of three α-helices flanked on two sides by anti-parallel β-sheets. Low order parameters as well as conformational exchanges in the centers of loop regions known as the DNA binding site and transcription site of HP-RRe suggested that flexibility of HP-RR e is essential for interaction with DNA. In conclusion, backbone dynamics information for HP-RR implies that structural flexibilities in HP-RRr are necessary for the phosphorylation site and the dynamic nature of HP-RRe is essential for the regulation of interaction between protein and DNA.
AB - An atypical orphan response regulator protein, HP1043 (HP-RR) in Helicobacter pylori, is proven to be essential for cell growth and does not require the well known phosphorelay scheme. HP-RR was identified as a symmetric dimer with two functional domains, an N-terminal regulatory domain (HP-RR r) and a C-terminal effector domain (HP-RRe). HP-RR is a new class of response regulator, as a phosphorylation-independent regulator. Previously, we have presented a detailed three-dimensional structure of HP-RR using NMR spectroscopy and X-ray crystallography. In this study, in order to understand the functional importance of flexibilities in HP-RRr and HP-RRe, T1, T2, heteronuclear NOE experiments have been performed and backbone dynamics of HP-RRr and HP-RR e were investigated. HP-RRr is a symmetric dimer and the interface region, α4-β5-α5 of dimer, showed high rigidity (high S 2 values). Site of rearrangements associated with phosphorylation of HP-RRr (Ser75: R ex = 3.382, Ile 95: R ex = 5.228) showed slow chemical exchanges. HP-RRe is composed of three α-helices flanked on two sides by anti-parallel β-sheets. Low order parameters as well as conformational exchanges in the centers of loop regions known as the DNA binding site and transcription site of HP-RRe suggested that flexibility of HP-RR e is essential for interaction with DNA. In conclusion, backbone dynamics information for HP-RR implies that structural flexibilities in HP-RRr are necessary for the phosphorylation site and the dynamic nature of HP-RRe is essential for the regulation of interaction between protein and DNA.
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U2 - 10.1007/s10059-013-2303-z
DO - 10.1007/s10059-013-2303-z
M3 - Article
C2 - 23456337
AN - SCOPUS:84879609949
VL - 35
SP - 158
EP - 165
JO - Molecules and Cells
JF - Molecules and Cells
SN - 1016-8478
IS - 2
ER -