The crytal structure of NGOO47 from Neisseria gonorrhoeae reveals a novel protein fold incorporating a helix-turn-helix motif

Proteins: Structure, Function and Bioinformatics

Volumn 78, Issue 7, 2010, Pages 1798-1802

  Ren, Jingshan ^a   Samshury, Sarah ^a,c   Nettleship, Joanne E ^a   Saunders, Nigel J ^b   Owens, Raymond J ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c UNIVERSITY OF MUNICH   (Germany)

Author keywords

Neisseria gonorrhoeae; Novel fold; Prophage; XRE family regulator

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; MOLECULAR CLONING; NEISSERIA GONORRHOEAE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STRUCTURE; CHEMICAL STRUCTURE; CHEMISTRY; DNA SEQUENCE; GENETIC DATABASE; GENETICS; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

NEISSERIA GONORRHOEAE;

BACTERIAL PROTEIN;

AMINO ACID MOTIFS; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; DATABASES, GENETIC; MODELS, MOLECULAR; NEISSERIA GONORRHOEAE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ANALYSIS, DNA;

MLCS; MLOWN;

EID: 77951245189     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22698     Document Type: Article

References (15)

1. Snyder LA, Davies JK, Ryan CS, Saunders NJ. Comparative overview of the genomic and genetic differences between the pathogenic Neisseria strains and species. Plasmid 2005;54:191-218.
2. Piekarowicz A, Klyz A, Majchrzak M, Adamczyk-Poplawska M, Maugel TK, Stein DC. Characterization of the dsDNA prophage sequences in the genome of Neisseria gonorrhoeae and visualization of productive bacteriophage. BMC Microbiol 2007;7:66.
3. Walhout AJ, Temple GF, Brasch MA, Hartley JL, Lorson MA, van den Heuvel S, Vidal M. GATEWAY recombinational cloning: application to the cloning of large numbers of open reading frames or ORFeomes. Methods Enzymol 2000;328:575-592.
4. Ren J, Nettleship JE, Sainsbury S, Saunders NJ, Owens RJ. Structure of the cold-shock domain protein from Neisseria meningitidis reveals a. strand-exchanged dimer. Acta Crystallogr Sect F Struct Biol Cryst Commun 2008;64:247-251.
5. Walter TS, Diprose JM, Mayo CJ, Siebold C, Pickford MG, Carter L, Sutton GC, Berrow NS, Brown J, Berry IM, Stewart-Jones GB, Grimes JM, Stammers DK, Esnouf RM, Jones EY, Owens RJ, Stuart Dl, Harlos K. A. procedure for setting up high-throughput nanolitre crystallization experiments. Crystallization workflow for initial screening, automated storage, imaging and optimization. Acta Crystallogr D-Biol Crystallogr 2005;61:651-657.
6. Terwilliger TC. Maximum-likelihood density modification. Acta Crystallogr D-Biol Crystallogr 2000;56:965-972.
7. Terwilliger TC, Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr D-Biol Crystallogr 1999;55:849-861.
8. Emsley P, Cowtan K, Coot: model-building tools for molecular graphics. Acta Crystallogr D-Biol Crystallogr 2004;60:2126-2132.
9. Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D-Biol Crystallogr 1997;53:240-255.
10. Bendtsen JD, Nielsen H, von Heijne G, Brunak S. Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 2004;340:783795.
11. Wood. HE, Devine KM, McConnell DJ. Characterisation of a repressor gene (xre) and a temperature-sensitive allele from the Bacillus subtilis prophage, PBSX. Gene 1990;96:83-88.
12. Wintjens R, Rooman M. Structural classification of HTH DNAbinding domains and protein-DNA interaction modes. J Mol Biol 1996;262:294-313.
13. Krissinel E, Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr 2004;60:2256-2268.
14. Holm L, Kaariainen S, Rosenstrom P, Schenkel A. Searching protein structure databases with DaliLite v.3. Bioinformatics 2008;24:27802781.
15. Veeramaiai M, Ye Y, Godzik A. TOPS++FATCAT: fast flexible structural alignment using constraints derived from TOPS+ Strings Model. BMC bioinformatics 2008:9:358.