Publication Date:
2004-10-02
Description:
Large RNA molecules, such as ribozymes, fold with well-defined tertiary structures that are important for their activity. There are many instances of ribozymes with identical function but differences in their secondary structures, suggesting alternative tertiary folds. Here, we report a crystal structure of the 161-nucleotide specificity domain of an A-type ribonuclease P that differs in secondary and tertiary structure from the specificity domain of a B-type molecule. Despite the differences, the cores of the domains have similar three-dimensional structure. Remarkably, the similar geometry of the cores is stabilized by a different set of interactions involving distinct auxiliary elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krasilnikov, Andrey S -- Xiao, Yinghua -- Pan, Tao -- Mondragon, Alfonso -- New York, N.Y. -- Science. 2004 Oct 1;306(5693):104-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15459389" target="_blank"〉PubMed〈/a〉
Keywords:
Base Sequence
;
Catalytic Domain
;
Conserved Sequence
;
Crystallography, X-Ray
;
Hydrogen Bonding
;
Models, Molecular
;
Molecular Sequence Data
;
Nucleic Acid Conformation
;
Phylogeny
;
RNA Precursors/chemistry/metabolism
;
RNA, Bacterial/*chemistry/metabolism
;
RNA, Transfer/chemistry/metabolism
;
Ribonuclease P/*chemistry/metabolism
;
Ribonucleotides/chemistry/metabolism
;
Thermus thermophilus/*chemistry/enzymology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
