3ZJ1

Structure of Nab2p tandem zinc finger 12

Summary for 3ZJ1

• Entry DOI: 10.2210/pdb3zj1/pdb
• Related: 3ZJ2
• NMR Information: BMRB: 18955
• Descriptor: NUCLEAR POLYADENYLATED RNA-BINDING PROTEIN NAB2, ZINC ION (2 entities in total)
• Functional Keywords: rna binding protein, ccch-type zinc finger, mrna export, poly(a) length control, polyadenosine rna binding.
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Nucleus: P32505
• Total number of polymer chains: 1
• Total formula weight: 9726.93

Authors

Martinez-Lumbreras, S.,Santiveri, C.M.,Mirassou, Y.,Zorrilla, S.,Perez-Canadillas, J.M. (deposition date: 2013-01-16, release date: 2013-09-11, Last modification date: 2024-05-15)

Primary citation

Martinez-Lumbreras, S.,Santiveri, C.M.,Mirassou, Y.,Zorrilla, S.,Perez-Canadillas, J.M.
Two Singular Types of Ccch Tandem Zinc Finger in Nab2P Contribute to Polyadenosine RNA Recognition.
Structure, 21:1800-, 2013

PubMed Abstract: The seven C-terminal CCCH-type zinc fingers of Nab2p bind the poly(A) tail of mRNA (∼A25). Using NMR, we demonstrated that the first four (Zf1-Zf4) contain two structurally independent tandems (TZF12 and TZF34) and bind A12 with moderate affinity (KD = 2.3 μM). Nab2p TZF12 contains a long α helix that contacts the zinc fingers Zf1 and Zf2 to arrange them similarly to Zf6-7 in the Nab2p Zf5-7 structure. Nab2p TZF34 exhibits a distinctive two-fold symmetry of the zinc centers with mutual recognition of histidine ligands. Our mutagenesis and NMR data demonstrate that the α helix of TZF12 and Zf3 of TZF34 define the RNA-binding interface, while Zf1, Zf2, and Zf4 seem to be excluded. These results further our understanding of polyadenosine RNA recognition by the CCCH domain of Nab2p. Moreover, we describe a hypothetical mechanism for controlling poly(A) tail length with specific roles for TZF12, TZF34, and Zf5-7 domains.

PubMed: 23994011
DOI: 10.1016/J.STR.2013.07.019

Experimental method

SOLUTION NMR