Biologie Digitale de l’ARN

@article{,

title = {Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices},

author = {C Charron and R Giege and B Lorber},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14684896},

isbn = {14684896},

year  = {2004},

date = {2004-01-01},

journal = {Acta Crystallogr D Biol Crystallogr},

volume = {60},

number = {Pt 1},

pages = {83-89},

abstract = {The intensely sweet protein thaumatin has been crystallized in a hexagonal lattice after a temperature shift from 293 to 277 K. The structure of the protein in the new crystal was solved at 1.6 A resolution. The protein fold is identical to that found in three other crystal forms grown in the presence of crystallizing agents of differing chemical natures. The proportions of lattice interactions involving hydrogen bonds, hydrophobic or ionic groups differ greatly from one form to another. Moreover, the distribution of acidic and basic residues taking part in contacts also varies. The hexagonal packing is characterized by the presence of channels parallel to the c axis that are so wide that protein molecules can diffuse through them.},

note = {0907-4449 

Journal Article},

keywords = {GIEGE  Comparative Study  Crystallization  Crystallography, Molecular  Plant Proteins/*chemistry  Support, Non-U.S. Gov't, Unité ARN, X-Ray  Hydrogen Bonding  Models},

pubstate = {published},

tppubtype = {article}

}

@article{,

title = {The crystal structure of UUCG tetraloop},

author = {E Ennifar and A Nikulin and S Tishchenko and A Serganov and N Nevskaya and M Garber and B Ehresmann and C Ehresmann and S Nikonov and P Dumas},

url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11071808},

isbn = {11071808},

year  = {2000},

date = {2000-01-01},

journal = {J Mol Biol},

volume = {304},

number = {1},

pages = {35-42},

abstract = {All large structured RNAs contain hairpin motifs made of a stem closed by several looped nucleotides. The most frequent loop motif is the UUCG one. This motif belongs to the tetraloop family and has the peculiarity of being highly thermodynamically stable. Here, we report the first crystal structure of two UUCG tetraloops embedded in a larger RNA-protein complex solved at 2.8 A resolution. The two loops present in the asymmetric unit are in a different crystal packing environment but, nevertheless, have an identical conformation. The observed structure is globally close to that obtained in solution by nuclear magnetic resonance. However, subtle differences point to a more detailed picture of the role played by 2'-hydroxyl groups in stabilising this tetraloop.},

note = {0022-2836 

Journal Article},

keywords = {16S/*chemistry/genetics/*metabolism  Ribosomal Proteins/chemistry/*metabolism  Solvents  Support, Base Sequence  Crystallography, Biomolecular  *Nucleic Acid Conformation  RNA Stability  RNA, ENNIFAR, Molecular  Molecular Sequence Data  Motion  Nuclear Magnetic Resonance, Non-U.S. Gov't  Thermodynamics, Ribosomal, Unité ARN, X-Ray  Hydrogen Bonding  Models},

pubstate = {published},

tppubtype = {article}

}