Crystal structure of E-coli YhbY:: A representative of a novel class of RNA binding proteins

被引:27
作者
Ostheimer, GJ
Barkan, A [1 ]
Matthews, BW
机构
[1] Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA
[2] Univ Oregon, Dept Chem, Eugene, OR 97403 USA
[3] Univ Oregon, Dept Biol, Eugene, OR 97403 USA
[4] Univ Oregon, Dept Phys, Eugene, OR 97403 USA
[5] Univ Oregon, Howard Hughes Med Inst, Eugene, OR 97403 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
D O I
10.1016/S0969-2126(02)00886-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
E. coli YhbY belongs to a conserved family of hypothetical proteins represented in eubacteria, archaea, and plants (Pfam code UPF0044). Three maize proteins harboring UPF0044-like domains are required for chloroplast group 11 intron splicing, and bioinformatic data suggest a role for prokaryotic UPF0044 members in translation. The crystal structure of YhbY has been determined. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome. Modeling studies indicate that the same surface is highly basic in all members of UPF0044, suggesting a conserved RNA binding surface. Taken together, the evidence suggests that members of UPF0044 constitute a previously unrecognized class of RNA binding domain.
引用
收藏
页码:1593 / 1601
页数:9
相关论文
共 42 条
[1]   Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation [J].
Allain, FHT ;
Gubser, CC ;
Howe, PWA ;
Nagai, K ;
Neuhaus, D ;
Varani, G .
NATURE, 1996, 380 (6575) :646-650
[2]   Analysis of the genome sequence of the flowering plant Arabidopsis thaliana [J].
Kaul, S ;
Koo, HL ;
Jenkins, J ;
Rizzo, M ;
Rooney, T ;
Tallon, LJ ;
Feldblyum, T ;
Nierman, W ;
Benito, MI ;
Lin, XY ;
Town, CD ;
Venter, JC ;
Fraser, CM ;
Tabata, S ;
Nakamura, Y ;
Kaneko, T ;
Sato, S ;
Asamizu, E ;
Kato, T ;
Kotani, H ;
Sasamoto, S ;
Ecker, JR ;
Theologis, A ;
Federspiel, NA ;
Palm, CJ ;
Osborne, BI ;
Shinn, P ;
Conway, AB ;
Vysotskaia, VS ;
Dewar, K ;
Conn, L ;
Lenz, CA ;
Kim, CJ ;
Hansen, NF ;
Liu, SX ;
Buehler, E ;
Altafi, H ;
Sakano, H ;
Dunn, P ;
Lam, B ;
Pham, PK ;
Chao, Q ;
Nguyen, M ;
Yu, GX ;
Chen, HM ;
Southwick, A ;
Lee, JM ;
Miranda, M ;
Toriumi, MJ ;
Davis, RW .
NATURE, 2000, 408 (6814) :796-815
[3]   THUMP - a predicted RNA-binding domain shared by 4-thiouridine, pseudouridine synthases and RNA methylases [J].
Aravind, L ;
Koonin, EV .
TRENDS IN BIOCHEMICAL SCIENCES, 2001, 26 (04) :215-217
[4]   THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].
BAILEY, S .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763
[5]   The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution [J].
Ban, N ;
Nissen, P ;
Hansen, J ;
Moore, PB ;
Steitz, TA .
SCIENCE, 2000, 289 (5481) :905-920
[6]   ALSCRIPT - A TOOL TO FORMAT MULTIPLE SEQUENCE ALIGNMENTS [J].
BARTON, GJ .
PROTEIN ENGINEERING, 1993, 6 (01) :37-40
[7]  
Bateman A, 2004, NUCLEIC ACIDS RES, V32, pD138, DOI [10.1093/nar/gkp985, 10.1093/nar/gkh121, 10.1093/nar/gkr1065]
[8]   X-RAY CRYSTALLOGRAPHY SHOWS THAT TRANSLATIONAL INITIATION-FACTOR IF3 CONSISTS OF 2 COMPACT ALPHA/BETA DOMAINS LINKED BY AN ALPHA-HELIX [J].
BIOU, V ;
SHU, F ;
RAMAKRISHNAN, V .
EMBO JOURNAL, 1995, 14 (16) :4056-4064
[9]   CONSERVED STRUCTURES AND DIVERSITY OF FUNCTIONS OF RNA-BINDING PROTEINS [J].
BURD, CG ;
DREYFUSS, G .
SCIENCE, 1994, 265 (5172) :615-621
[10]  
Cowtan K., 1994, JOINT CCP4 ESF EACBM, V31, P34