1SRK

Solution structure of the third zinc finger domain of FOG-1

Summary for 1SRK

• Entry DOI: 10.2210/pdb1srk/pdb
• NMR Information: BMRB: 6216
• Descriptor: Zinc finger protein ZFPM1, ZINC ION (2 entities in total)
• Functional Keywords: classical zinc finger, transcription
• Biological source: Mus musculus (house mouse)
• Cellular location: Nucleus: O35615
• Total number of polymer chains: 1
• Total formula weight: 3879.88

Authors

Simpson, R.J.Y.,Lee, S.H.Y.,Bartle, N.,Matthews, J.M.,Mackay, J.P.,Crossley, M. (deposition date: 2004-03-22, release date: 2004-09-21, Last modification date: 2024-05-22)

Primary citation

Simpson, R.J.Y.,Lee, S.H.Y.,Bartle, N.,Sum, E.Y.,Visvader, J.E.,Matthews, J.M.,Mackay, J.P.,Crossley, M.
A Classic Zinc Finger from Friend of GATA Mediates an Interaction with the Coiled-coil of Transforming Acidic Coiled-coil 3.
J.Biol.Chem., 279:39789-39797, 2004

PubMed Abstract: Classic zinc finger domains (cZFs) consist of a beta-hairpin followed by an alpha-helix. They are among the most abundant of all protein domains and are often found in tandem arrays in DNA-binding proteins, with each finger contributing an alpha-helix to effect sequence-specific DNA recognition. Lone cZFs, not found in tandem arrays, have been postulated to function in protein interactions. We have studied the transcriptional co-regulator Friend of GATA (FOG), which contains nine zinc fingers. We have discovered that the third cZF of FOG contacts a coiled-coil domain in the centrosomal protein transforming acidic coiled-coil 3 (TACC3). Although FOG-ZF3 exhibited low solubility, we have used a combination of mutational mapping and protein engineering to generate a derivative that was suitable for in vitro and structural analysis. We report that the alpha-helix of FOG-ZF3 recognizes a C-terminal portion of the TACC3 coiled-coil. Remarkably, the alpha-helical surface utilized by FOG-ZF3 is the same surface responsible for the well established sequence-specific DNA-binding properties of many other cZFs. Our data demonstrate the versatility of cZFs and have implications for the analysis of many as yet uncharacterized cZF proteins.

PubMed: 15234987
DOI: 10.1074/jbc.M404130200

Experimental method

SOLUTION NMR