The bridge helix coordinates movements of modules in RNA polymerase

Autor:	Pyae P Hein, Robert Landick
Jazyk:	angličtina
Rok vydání:	2010
Předmět:	Models Molecular Physiology Base pair 5.8S ribosomal RNA Molecular Sequence Data Plant Science Biology General Biochemistry Genetics and Molecular Biology Catalysis Protein Structure Secondary chemistry.chemical_compound Protein structure Structural Biology Transcription (biology) RNA polymerase Catalytic Domain RNA polymerase I natural sciences Amino Acid Sequence lcsh:QH301-705.5 Ecology Evolution Behavior and Systematics Polymerase Genetics Agricultural and Biological Sciences(all) Biochemistry Genetics and Molecular Biology(all) Nucleic acid sequence Cell Biology DNA-Directed RNA Polymerases Cell biology Protein Structure Tertiary chemistry lcsh:Biology (General) biology.protein Commentary General Agricultural and Biological Sciences Developmental Biology Biotechnology
Zdroj:	BMC Biology, Vol 8, Iss 1, p 141 (2010) BMC Biology
ISSN:	1741-7007
Popis:	The RNA polymerase 'bridge helix' is a metastable α-helix that spans the leading edge of the enzyme active-site cleft. A new study published in BMC Biology reveals surprising tolerance to helix-disrupting changes in a region previously thought crucial for translocation, and suggests roles for two hinge-like segments of the bridge helix in coordinating modules that move during the nucleotide-addition cycle. See Research article: http://www.biomedcentral.com/1741-7007/8/134
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4059fe2b425d12cb2389a137e73c0ae2 http://www.biomedcentral.com/1741-7007/8/141 Zobrazit plný text záznamu Full text from SpringerLink