Crystal structure of TTHA1657 (AT-Rich DNA-binding protein; p25) from Thermus thermophilus HB8 at 2.16 A° resolution

Proteins: Structure, Function and Genetics

Volumn 66, Issue 3, 2007, Pages 755-759

  Nakamura, Akira ^a   Sosa, Akira ^a   Komori, Hirofumi ^a   Kita, Akiko ^a   Miki, Kunio ^a,b  

^a KYOTO UNIVERSITY   (Japan)

^b Harima Institute ^*  (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; PROTEIN P25;

CONFERENCE PAPER; CRYSTAL STRUCTURE; GENE; NONHUMAN; NUCLEOTIDE SEQUENCE; OPTICAL RESOLUTION; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTEIN STRUCTURE; THERMUS THERMOPHILUS; TTHA1657 GENE;

BASE SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DNA PRIMERS; DNA-BINDING PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; THERMUS THERMOPHILUS;

THERMUS THERMOPHILUS;

EID: 33846202958     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21222     Document Type: Conference Paper

References (22)

1. Du X, Péne J. Identification, cloning and expression of p25, an AT-rich DNA-binding protein from the extreme thermophile, Thermus aquaticus YT-1. Nucleic Acids Res 1999;27:1690-1697.
2. + redox poise in Streptomyces coelicolor A3(2). EMBO J 2003;22:4856-4865.
3. Sickmier EA, Brekasis D, Paranawithana S, Bonanno JB, Paget MSB, Burley SK, Kielkopf CL. X-ray structure of a Rex-family repressor/NADH complex insights into the mechanism of redox sensing. Structure 2005;13:43-54.
4. Dauter Z, Dauter M, Rajashankar R. Novel approach to phasing proteins: derivatization by short cryo-soaking with halides. Acta Crystallogr D 2000;56:232-237.
5. Nagem RAP, Dauter Z, Polikarpov I. Protein crystal structure solution by fast incorporation of negatively and positively charged anomalous scatterers. Acta Crystallogr D 2001;57:996-1002.
6. Green DW, Ingram VM, Perutz F. The structure of haemoglobin IV. Sign determination by the isomorphous replacement method. Proc R Soc London Ser A 1954;225:287-307.
7. Bragg WL, Perutz F. The structure of haemoglobin: Fourier projections on the 010 plane. Proc R Soc London Ser A 1954;225:315.
8. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1991;276:307-325.
9. Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 1994;50:760-763.
10. Terwilliger TC, Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr D 1999;55:849-861.
11. Terwilliger TC. Maximum-likelihood density modification. Acta Crystallogr D 2000;56:965-972.
12. Perrakis A, Morris R, Lamzin VS. Automated protein model building combined with iterative structure refinement. Nat Struct Biol 1999;6:458-463.
13. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
14. Brünger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL. Crystallography & NMR System: a new software suite for macromolecular structure determination. Acta Crystallogr D 1998;54:905-921.
15. Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst 1991;24:946-950.
16. Merritt EA, Bacon DJ. Raster3D: photorealistic molecular graphics. Methods Enzymol 1997;277:505-524.
17. Lawrence MC, Bourke P. CONSCRIPT: a program for generating electron density isosurfaces for presentation in protein crystallography. J Appl Cryst 2000;33:990-991.
18. Gouet P, Courcelle E, Stuart DI, Métoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999;15:305-308.
19. Gajiwara KS, Burley SK. Winged helix proteins. Curr Opin Struct Biol 2000;10:110-116.
20. Lesk AM. NAD-binding domains of dehydrogenases. Curr Opin Struct Biol 1995;5:775-783.
21. Rao ST, Rossmann MG. Comparison of super-secondary structures in proteins. J Mol Biol 1973;76:241-256.
22. Schau M, Chen Y, Hulett FM. Bacillus subtilis Ydi H is a direct negative regulator of the cyd ABCD operon. J Bacteriol 2004;186:4585-4595.