Structural analysis of the transcriptional regulator homolog protein from Pyrococcus horikoshii OT3

Proteins: Structure, Function and Genetics

Volumn 63, Issue 4, 2006, Pages 1084-1086

  Okada, Ui ^a   Sakai, Naoki ^a   Yao, Min ^a   Watanabe, Nobuhisa ^a   Tanaka, Isao ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; MULTIDRUG RESISTANCE PROTEIN; REGULATOR PROTEIN;

ARTICLE; CRYSTALLOGRAPHY; GEL PERMEATION CHROMATOGRAPHY; GENE; LIGHT SCATTERING; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN STRUCTURE; PYROCOCCUS HORIKOSHII; TRANSCRIPTION REGULATION; X RAY DIFFRACTION;

PYROCOCCUS HORIKOSHII;

EID: 33646815967     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20913     Document Type: Article

References (18)

1. Kawarabayasi Y, Sawada M, Horikawa H, Haikawa Y, Hino Y, Yamamoto S, Sekine M, Baba S, Kosugi H, Hosoyama A, Nagai Y, Sakai M, Ogura K, Otsuka R, Nakazawa H, Takamiya M, Ohfuku Y, Funahashi T, Tanaka T, Kudoh Y, Yamazaki J, Kushida N, Oguchi A, Aoki K, Kikuchi H. Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3. DNA Res 1998;5:55-76.
2. Bateman A, Coin L, Durbin R, Finn RD, Hollich V, Griffiths-Jones S, Khanna A, Marshall M, Moxon S, Sonnhammer EL, Studholme DJ, Yeats C, Eddy SR. The Pfam protein families database. Nucleic Acids Res 2004;32(Database issue):D138-D141.
3. Busenlehner LS, Pennella MA, Giedroc DP. The SmtB/ArsR family of metalloregulatory transcriptional repressors: structural insights into prokaryotic metal resistance. FEMS Microbiol Rev 2003;27:131-143.
4. Eicken C, Pennella MA, Chen X, Koshlap KM, VanZile ML, Sacchettini JC, Giedroc DP. A metal-ligand-mediated intersub-unit allosteric switch in related SmtB/ArsR zinc sensor proteins. J Mol Biol 2003;333:683-695.
5. Cook WJ, Kar SR, Taylor KB, Hall LM. Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins. J Mol Biol 1998;275:337-346.
6. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326.
7. Terwilliger TC, Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr D Biol Crystallogr 1999;55(Pt 4):849-861.
8. Terwilliger TC. Reciprocal-space solvent flattening. Acta Crystallogr D Biol Crystallogr 1999;55:1863-1871.
9. Lamzin VS, Wilson KS. Automated refinement of protein models. Acta Crystallogr D Biol Crystallogr 1993;49(Pt 1):129-147.
10. 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(Pt 2):110-119.
11. Brunger 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 Biol Crystallogr 1998;54(Pt 5):905-921.
12. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE. The Protein Data Bank. Nucleic Acids Res 2000;28:235-242.
13. Holm L, Sander C. Touring protein fold space with Dali/FSSP. Nucleic Acids Res 1998;26:316-319.
14. Alekshun MN, Levy SB, Mealy TR, Seaton BA, Head JF. The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution. Nat Struct Biol 2001;8:710-714.
15. Grkovic S, Brown MH, Skurray RA. Regulation of bacterial drug export systems. Microbiol Mol Biol Rev 2002;66:671-701, table of contents.
16. Schumacher MA, Brennan RG. Structural mechanisms of multidrug recognition and regulation by bacterial multidrug transcription factors. Mol Microbiol 2002;45:885-893.
17. Tuerk C, Gold L. Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science 1990;249:505-510.
18. Ellington AD, Szostak JW. In vitro selection of RNA molecules that bind specific ligands. Nature 1990;346:818-822.