This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3qhs
From Proteopedia
Crystal structure of full-length Hfq from Escherichia coli
Structural highlights
FunctionHFQ_ECOLI RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Involved in the regulation of stress responses mediated by the sigma factors RpoS, sigma-E and sigma-32. Binds with high specificity to tRNAs. In vitro, stimulates synthesis of long tails by poly(A) polymerase I. Required for RNA phage Qbeta replication.[1] [2] [3] [4] [5] Seems to play a role in persister cell formation; upon overexpression decreases persister cell formation while deletion increases persister formation.[6] [7] [8] [9] [10] Publication Abstract from PubMedThe structure of full-length host factor Qbeta (Hfq) from Escherichia coli obtained from a crystal belonging to space group P1, with unit-cell parameters a = 61.91, b = 62.15, c = 81.26 A, alpha = 78.6, beta = 86.2, gamma = 59.9 degrees , was solved by molecular replacement to a resolution of 2.85 A and refined to R(work) and R(free) values of 20.7% and 25.0%, respectively. Hfq from E. coli has previously been crystallized and the structure has been solved for the N-terminal 72 amino acids, which cover approximately 65% of the full-length sequence. Here, the purification, crystallization and structural data of the full 102-amino-acid protein are presented. These data revealed that the presence of the C-terminus changes the crystal packing of E. coli Hfq. The crystal structure is discussed in the context of the recently published solution structure of Hfq from E. coli. Structural analysis of full-length Hfq from Escherichia coli.,Beich-Frandsen M, Vecerek B, Sjoblom B, Blasi U, Djinovic-Carugo K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt, 5):536-40. Epub 2011 Apr 20. PMID:21543856[11] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||
