Access the full text.
Sign up today, get DeepDyve free for 14 days.
H. Hegyi, M. Gerstein (1999)
The relationship between protein structure and function: a comprehensive survey with application to the yeast genome.Journal of molecular biology, 288 1
P. Bork, E. Koonin (1998)
Predicting functions from protein sequences—where are the bottlenecks?Nature Genetics, 18
Yokoyama (2000)
943Nature Struct. Biol., 7
Anne Neuenfeldt, A. Just, H. Betat, M. Mörl (2008)
Evolution of tRNA nucleotidyltransferases: A small deletion generated CC-adding enzymesProceedings of the National Academy of Sciences, 105
L. Aravind, E. Koonin (1999)
DNA polymerase beta-like nucleotidyltransferase superfamily: identification of three new families, classification and evolutionary history.Nucleic acids research, 27 7
B. Matthews (1968)
Solvent content of protein crystals.Journal of molecular biology, 33 2
P. Bralley, Samantha Chang, George Jones (2005)
A Phylogeny of Bacterial RNA Nucleotidyltransferases: Bacillus halodurans Contains Two tRNA NucleotidyltransferasesJournal of Bacteriology, 187
A. Vagin, A. Teplyakov (2010)
Molecular replacement with MOLREP.Acta crystallographica. Section D, Biological crystallography, 66 Pt 1
Lars Pedersen, M. Benning, Hazel Holden (1995)
Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase.Biochemistry, 34 41
L. Holm, C. Sander (1995)
DNA polymerase β belongs to an ancient nucleotidyltransferase superfamilyTrends in Biochemical Sciences, 20
H. Betat, Christiane Rammelt, M. Mörl (2010)
tRNA nucleotidyltransferases: ancient catalysts with an unusual mechanism of polymerizationCellular and Molecular Life Sciences, 67
M. Winn, C. Ballard, K. Cowtan, E. Dodson, P. Emsley, P. Evans, R. Keegan, E. Krissinel, A. Leslie, A. Mccoy, S. McNicholas, G. Murshudov, N. Pannu, E. Potterton, H. Powell, R. Read, A. Vagin, K. Wilson (2011)
Overview of the CCP4 suite and current developmentsActa Crystallographica Section D: Biological Crystallography, 67
A. Mccoy, R. Grosse-Kunstleve, P. Adams, M. Winn, L. Storoni, R. Read (2007)
Phaser crystallographic softwareJournal of Applied Crystallography, 40
C. Lehmann, S. Pullalarevu, W. Krajewski, M. Willis, A. Galkin, A. Howard, O. Herzberg (2005)
Structure of HI0073 from Haemophilus influenzae, the nucleotide‐binding domain of a two‐protein nucleotidyl transferaseProteins: Structure, 60
N. Manoj, E. Strauss, T. Begley, S. Ealick (2003)
Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution.Structure, 11 8
R. Keegan, M. Winn (2007)
Automated search-model discovery and preparation for structure solution by molecular replacement.Acta crystallographica. Section D, Biological crystallography, 63 Pt 4
C. Chothia, A. Lesk (1986)
The relation between the divergence of sequence and structure in proteins.The EMBO Journal, 5
S. Yokoyama, Y. Matsuo, H. Hirota, T. Kigawa, M. Shirouzu, Y. Kuroda, Hitoshi Kurumizaka, Shinichi Kawaguchi, Yutaka Ito, Takehiko Shibata, Masatsune Kainosho, Y. Nishimura, Yorinao Inoue, S. Kuramitsu (2000)
Structural genomics projects in Japan.Progress in biophysics and molecular biology, 73 5
Z. Otwinowski, W. Minor (1997)
[20] Processing of X-ray diffraction data collected in oscillation mode.Methods in enzymology, 276
R. Salinas, C. Camilo, Simona Tomaselli, E. Valencia, C. Farah, H. El-Dorry, F. Chambergo (2009)
Solution structure of the C‐terminal domain of multiprotein bridging factor 1 (MBF1) of Trichoderma reeseiProteins: Structure, 75
The TTHA1015 gene from Thermus thermophilus HB8 encodes a hyperthermophilic nucleotidyltransferase. TTHA1015 has high homology to proteins belonging to two related families: the nucleotidyltransferase‐domain superfamily and the DNA polymerase β‐like family. However, no crystal structures of these proteins have been reported. Determination of the crystal structure of TTHA1015 will help in elucidation of its function and will be useful for understanding the relationship between the structure and the function of these homologous proteins. In this study, TTHA1015 was expressed, purified and crystallized. X‐ray diffraction data were collected to 1.70 Å resolution. The crystal belonged to the monoclinic space group C2, with unit‐cell parameters a = 65.5, b = 34.7, c = 42.4 Å, β = 119.1°. There was one molecule per asymmetric unit, giving a Matthews coefficient of 1.86 Å3 Da−1 and an approximate solvent content of 34%.
Acta Crystallographica Section F – Wiley
Published: Jul 1, 2011
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.