1ZFD

SWI5 ZINC FINGER DOMAIN 2, NMR, 45 STRUCTURES

Summary for 1ZFD

• Entry DOI: 10.2210/pdb1zfd/pdb
• Descriptor: SWI5, ZINC ION (2 entities in total)
• Functional Keywords: dna binding motif, zinc finger dna binding domain
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P08153
• Total number of polymer chains: 1
• Total formula weight: 3865.68

Authors

Neuhaus, D.,Nakaseko, Y.,Schwabe, J.W.R.,Rhodes, D.,Klug, A. (deposition date: 1996-04-04, release date: 1996-10-14, Last modification date: 2024-05-22)

Primary citation

Neuhaus, D.,Nakaseko, Y.,Schwabe, J.W.,Klug, A.
Solution structures of two zinc-finger domains from SWI5 obtained using two-dimensional 1H nuclear magnetic resonance spectroscopy. A zinc-finger structure with a third strand of beta-sheet.
J.Mol.Biol., 228:637-651, 1992

PubMed Abstract: This paper describes the detailed three-dimensional structures of two zinc-finger domains from the yeast transcription factor SWI5, calculated using the results of the n.m.r. experiments described in the accompanying paper. The structure of finger 2 is essentially similar to those previously obtained by others for isolated, synthetic single zinc-finger domains in solution, and for the three zinc-finger peptide Zif268 in its crystalline complex with DNA. The N-terminal half of the sequence forms a two-stranded, irregular beta-sheet containing both of the metal-binding cysteine residues, while the remainder of the structure forms a helix. Approximately the first half of this helix is alpha-helical, whereas the C-terminal portion, including the two metal-binding histidine residues, is 3(10) helical. Four invariant hydrophobic residues form a core to the structure. In contrast to all previously described structures of zinc-finger domains, finger 1 has an additional strand in the beta-sheet, formed by residues N-terminal to the formal start of the finger motif. This additional strand plays a role in stabilising the folded form of finger 1, since a two-finger peptide lacking the N-terminal residues showed folded structure in finger 2 but not in finger 1.

PubMed: 1453468
DOI: 10.1016/0022-2836(92)90846-C

Experimental method

SOLUTION NMR