title: Backbone resonance assignments of the Escherichia coli 62 kDa protein, Hsp31.
abstract: Dimeric Hsp31 protein was first characterized as a holding chaperone of Escherichia coli (E. coli), and has been suggested as having protease activity due to the presence of a potential catalytic triad, Cys185, His186, and Asp214. However, it has recently been reported that Hsp31 displays a relatively strong glyoxalase III activity that can decompose reactive carbonyl species (methylglyoxal and glyoxal) in the absence of additional cofactor. Hsp31 is a representative member of the DJ-1/ThiJ/PfpI protein superfamily, and the importance of DJ-1 protein in Parkinson's disease has been well known. The structural flexibility of the long loop region, which encompasses from the P- to the A-domain, is important for the chaperone activity of Hsp31. The backbone chemical shifts (CSs) would be useful for studying the structural changes of Hsp31 that are critical for the holding chaperone activity, and also for deciphering the switching mechanism between the glyoxalase III and the chaperone. Here, we report the backbone CSs (HN, N, CO, Cα, and Cβ) of the deuterated Hsp31 protein (62 kDa). The CS analysis showed that the predicted regions of secondary structures are in good agreement with those observed in the previous crystal structure of Hsp31.
authors.affiliation: Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 291 Daehak-Ro, Yuseong-Gu, Daejeon, 34141, Republic of Korea.|Protein Structure Group, Korea Basic Science Institute, 162 Yeongudanji-Ro, Ochang-Eup, Cheongju-Si, Chungcheongbuk-Do, 28119, Republic of Korea.
authors.forename: Jihong
authors.initials: J
authors.lastname: Kim
authors.affiliation: Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 291 Daehak-Ro, Yuseong-Gu, Daejeon, 34141, Republic of Korea.|Protein Structure Group, Korea Basic Science Institute, 162 Yeongudanji-Ro, Ochang-Eup, Cheongju-Si, Chungcheongbuk-Do, 28119, Republic of Korea.|New Drug Development Center, Osong Medical Innovation Foundation, 123 Osongsaengmyeong-Ro, Osong-Eup, Heungdeok-Gu, Cheongju-Si, Chungcheongbuk-Do, 28160, Republic of Korea.
authors.forename: Dongwook
authors.initials: D
authors.lastname: Choi
authors.affiliation: Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 291 Daehak-Ro, Yuseong-Gu, Daejeon, 34141, Republic of Korea.
authors.forename: Chankyu
authors.initials: C
authors.lastname: Park
authors.affiliation: Protein Structure Group, Korea Basic Science Institute, 162 Yeongudanji-Ro, Ochang-Eup, Cheongju-Si, Chungcheongbuk-Do, 28119, Republic of Korea. ksryu@kbsi.re.kr.|Department of Bio-Analytical Science, University of Science and Technology, 217 Gajeong-Ro, Yuseong-Gu, Daejon, 34113, Republic of Korea. ksryu@kbsi.re.kr.
authors.forename: Kyoung-Seok
authors.initials: KS
authors.lastname: Ryu
mesh_terms: D029968:Escherichia coli Proteins / Q000737:chemistry*; D018832:Molecular Chaperones / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular
chemical_list: D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; C469996:hchA protein, E coli
keywords: Backbone chemical shift assignment; Heteronuclear NMR; Hsp31; TROSY