Structure of HI1333 (YhbY), a putative RNA-binding protein from Haemophilus influenzae

Proteins: Structure, Function and Genetics

Volumn 49, Issue 3, 2002, Pages 423-426

  Willis, Mark A ^a   Krajewski, Wojciech ^a   Chalamasetty, Vani Rao ^b   Reddy, Prasad ^b   Howard, Andrew ^c,d   Herzberg, Osnat ^a  

^a UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE   (United States)

^b NATIONAL INSTITUTE OF STANDARDS AND TECHNOLOGY   (United States)

^c ARGONNE NATIONAL LABORATORY   (United States)

^d ILLINOIS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN HI1333; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENE; CRYSTAL STRUCTURE; GENETIC CODE; HAEMOPHILUS INFLUENZAE; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN ISOLATION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

CRYSTALLOGRAPHY, X-RAY; HAEMOPHILUS INFLUENZAE; MODELS, MOLECULAR; RNA-BINDING PROTEINS;

BACTERIA (MICROORGANISMS); HAEMOPHILUS; HAEMOPHILUS INFLUENZAE;

EID: 0037110588     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10225     Document Type: Article

References (17)

1. Draper DE. Themes in RNA-protein recognition. J Mol Biol 1999;293:255-270.
2. Reddy P, Peterkofsky A, McKenney K. Hyperexpression and purification of Escherichia coli adenylate cyclase using a vector designed for expression of lethal gene products. Nucleic Acids Res 1989;17:10473-10488.
3. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326.
4. Terwilliger TC, Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr D Biol Crystallogr 1999;55:849-861.
5. Sheldrick GM. XPREP Programm zur Datenanalyse: Universität Göttingen; 1997.
6. Brünger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 1998;54:905-921.
7. Terwilliger TC. Maximum-likelihood density modification. Acta Crystallogr D Biol Crystallogr 2000;56:965-972.
8. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
9. Sheldrick GM, Schneider TR. SHELXL: High resolution refinement. Methods Enzymol 1997;277:319-343.
10. Laskowski RA, Macarthur MW, Moss DS, Thornton JM. Pro-check - A program to check the stereochemical quality of protein structures. J Appl Crystallogr 1993;26:283-291.
11. Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ. Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res 1997;25: 3389-402.
12. Till B, Schmitz-Linneweber C, Williams-Carrier R, Barkan A. CRS1 is a novel group II intron splicing factor that was derived from a domain of ancient origin. RNA 2001;7:1227-1238.
13. Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
14. Biou V, Shu F, Ramakrishnan V. X-ray crystallography shows that translational initiation factor IF3 consists of two compact alpha/beta domains linked by an alpha-helix. Embo J 1995;14:4056-4064.
15. Katoh E, Hatta T, Shindo H, Ishii Y, Yamada H, Mizuno T, Yamazaki T. High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division. J Mol Biol 2000;304:219-229.
16. Grishin NV. KH domain: One motif, two folds. Nucleic Acids Res 2001;29:638-643.
17. Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 2000;408:796-815.