2HGH

Transcription Factor IIIA zinc fingers 4-6 bound to 5S rRNA 55mer (NMR structure)

Summary for 2HGH

• Entry DOI: 10.2210/pdb2hgh/pdb
• Related: 1TF3 1ZNF
• NMR Information: BMRB: 7194
• Descriptor: 55-MER, Transcription factor IIIA, ZINC ION (3 entities in total)
• Functional Keywords: zinc finger, transcription-rna complex, transcription/rna
• Biological source: Xenopus laevis (African clawed frog); More
• Cellular location: Nucleus: P03001
• Total number of polymer chains: 2
• Total formula weight: 28122.48

Authors

Lee, B.M. (deposition date: 2006-06-27, release date: 2006-08-01, Last modification date: 2024-05-29)

Primary citation

Lee, B.M.,Xu, J.,Clarkson, B.K.,Martinez-Yamout, M.A.,Dyson, J.H.,Case, D.A.,Gottesfeld, J.M.,Wright, P.E.
Induced Fit and 'Lock and Key' Recognition of 5 S RNA by Zinc Fingers of Transcription Factor IIIA
J.Mol.Biol., 357:275-291, 2006

PubMed Abstract: Transcription factor IIIA (TFIIIA) is a Cys2His2 zinc finger protein that regulates expression of the 5 S ribosomal RNA gene by binding specifically to the internal control element. TFIIIA also functions in transport and storage of 5 S RNA by binding directly to the RNA transcript. To obtain insights into the mechanism by which TFIIIA recognizes 5 S RNA, we determined the solution structure of the middle three zinc fingers bound to the central core of 5 S RNA. Finger 4 utilizes "lock and key" recognition to bind in the widened major groove of the pre-structured RNA loop E motif. This interaction is mediated by direct hydrogen bonding interactions with bases. In contrast, recognition of loop A, a flexible junction of three helices, occurs by an induced fit mechanism that involves reorganization of the conserved CAUA motif and structuring of the finger 5-finger 6 interface to form a complementary RNA binding surface.

PubMed: 16405997
DOI: 10.1016/j.jmb.2005.12.010

Experimental method

SOLUTION NMR