TY - JOUR
T1 - Solution structure of the mouse enhancer of rudimentary protein reveals a novel fold
AU - Li, Hua
AU - Inoue, Makoto
AU - Yabuki, Takashi
AU - Aoki, Masaaki
AU - Seki, Eiko
AU - Matsuda, Takayoshi
AU - Nunokawa, Emi
AU - Motoda, Yoko
AU - Kobayashi, Atsuo
AU - Terada, Takaho
AU - Shirouzu, Mikako
AU - Koshiba, Seizo
AU - Lin, Yi Jan
AU - Güntert, Peter
AU - Suzuki, Harukazu
AU - Hayashizaki, Yoshihide
AU - Kigawa, Takanori
AU - Yokoyama, Shigeyuki
N1 - Funding Information:
The authors thank Yukiko Fujikura, Natsuko Matsuda, Miyuki Saito, Yukako Miyata, Masaomi Ikari, Fumiko Hiroyasu, Yasuko Tomo, Megumi Watanabe, Miyuki Sato, Satoko Yasuda, Hiroshi Hirota, and Mayumi Yoshida for help with sample preparations and maintaining the NMR facility. This work was supported by the RIKEN Structural Genomics/Proteomics Initiative (RSGI), the National Project on Protein Structural and Functional Analyses, Ministry of Education, Culture, Sports, Science and Technology of Japan.
PY - 2005/8
Y1 - 2005/8
N2 - In summary, the ER protein, which is highly conserved among organisms as diverse as vertebrates, invertebrates, and plants, has been implicated as functioning in pyrimidine biosynthesis and the cell cycle. In this study, ER was found to behave as a dimer in solution, and the solution structure of the ER monomer was determined by heteronuclear NMR spectroscopy. The ER monomer consists of a four-stranded antiparallel b-sheet, with a strand order of β2β1β3β4, and three a-helices (α1, α2, and α3) packed against one side of the sheet, with an overall topology of β1β2α1α2β3β4α3. A structural homology search revealed that ER forms a novel fold. These structural features of ER will shed light on its functional mechanism at the molecular level. The coordinates have been deposited in the Pro tein Data Bank (accession code 1WWQ).
AB - In summary, the ER protein, which is highly conserved among organisms as diverse as vertebrates, invertebrates, and plants, has been implicated as functioning in pyrimidine biosynthesis and the cell cycle. In this study, ER was found to behave as a dimer in solution, and the solution structure of the ER monomer was determined by heteronuclear NMR spectroscopy. The ER monomer consists of a four-stranded antiparallel b-sheet, with a strand order of β2β1β3β4, and three a-helices (α1, α2, and α3) packed against one side of the sheet, with an overall topology of β1β2α1α2β3β4α3. A structural homology search revealed that ER forms a novel fold. These structural features of ER will shed light on its functional mechanism at the molecular level. The coordinates have been deposited in the Pro tein Data Bank (accession code 1WWQ).
KW - Enhancer of rudimentary
KW - NMR structure
KW - Pyrimidine biosynthesis
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U2 - 10.1007/s10858-005-7959-z
DO - 10.1007/s10858-005-7959-z
M3 - Article
C2 - 16211485
AN - SCOPUS:27244452100
SN - 0925-2738
VL - 32
SP - 329
EP - 334
JO - Journal of Biomolecular NMR
JF - Journal of Biomolecular NMR
IS - 4
ER -