1A5J

CHICKEN B-MYB DNA BINDING DOMAIN, REPEAT 2 AND REPEAT3, NMR, 32 STRUCTURES

Summary for 1A5J

• Entry DOI: 10.2210/pdb1a5j/pdb
• NMR Information: BMRB: 4114,5517
• Descriptor: B-MYB (1 entity in total)
• Functional Keywords: dna-binding protein, protooncogene product, dna binding protein
• Biological source: Gallus gallus (chicken)
• Cellular location: Nucleus: Q03237
• Total number of polymer chains: 1
• Total formula weight: 12958.92

Authors

Mcintosh, P.B.,Carr, M.D.,Wollborn, U.,Frenkiel, T.A.,Feeney, J.,Mccormick, J.E.,Klempnauer, K.H. (deposition date: 1998-02-16, release date: 1998-07-01, Last modification date: 2024-05-22)

Primary citation

McIntosh, P.B.,Frenkiel, T.A.,Wollborn, U.,McCormick, J.E.,Klempnauer, K.H.,Feeney, J.,Carr, M.D.
Solution structure of the B-Myb DNA-binding domain: a possible role for conformational instability of the protein in DNA binding and control of gene expression.
Biochemistry, 37:9619-9629, 1998

PubMed Abstract: Double- and triple-resonance heteronuclear NMR spectroscopy have been used to determine the high-resolution solution structure of the minimal B-Myb DNA-binding domain (B-MybR2R3) and to characterize the specific complex formed with a synthetic DNA fragment corresponding to the Myb target site on the Myb-regulated gene tom-1. B-MybR2R3 is shown to consist of two independent protein domains (R2 and R3) joined by a short linker, which have strikingly different tertiary structures despite significant sequence similarities. In addition, the C-terminal region of B-Myb R2 is confirmed to have a poorly defined structure, reflecting the existence of multiple conformations in slow to intermediate exchange. This contrasts with the tertiary structure reported for c-MybR2R3, in which both R2 and R3 have the same fold and the C-terminal region of R2 forms a stable, well-defined helix [Ogata, K., et al. (1995) Nat. Struct. Biol. 2, 309-320]. The NMR data suggest there are extensive contacts between B-MybR2R3 and its DNA target site in the complex and are consistent with a significant conformational change in the protein on binding to DNA, with one possibility being the formation of a stable helix in the C-terminal region of R2. In addition, conformational heterogeneity identified in R2 of B-MybR2R3 bound to the tom-1-A target site may play an important role in the control of gene expression by Myb proteins.

PubMed: 9657674
DOI: 10.1021/bi972861z

Experimental method

SOLUTION NMR