1ZFO

AMINO-TERMINAL LIM-DOMAIN PEPTIDE OF LASP-1, NMR

Summary for 1ZFO

• Entry DOI: 10.2210/pdb1zfo/pdb
• Descriptor: LASP-1, ZINC ION (2 entities in total)
• Functional Keywords: lim domain, zinc-finger, metal-binding protein, metal binding protein
• Biological source: Sus scrofa (pig)
• Cellular location: Cytoplasm, cell cortex (By similarity): P80171
• Total number of polymer chains: 1
• Total formula weight: 3614.65

Authors

Hammarstrom, A.,Berndt, K.D.,Sillard, R.,Adermann, K.,Otting, G. (deposition date: 1996-05-06, release date: 1996-11-08, Last modification date: 2024-11-20)

Primary citation

Hammarstrom, A.,Berndt, K.D.,Sillard, R.,Adermann, K.,Otting, G.
Solution structure of a naturally-occurring zinc-peptide complex demonstrates that the N-terminal zinc-binding module of the Lasp-1 LIM domain is an independent folding unit.
Biochemistry, 35:12723-12732, 1996

PubMed Abstract: The three-dimensional solution structure of the 1:1 complex between the synthetic peptide ZF-1 and zinc was determined by 1H NMR spectroscopy. The peptide, initially isolated from pig intestines, is identical in sequence to the 30 N-terminal amino acid residues of the human protein Lasp-1 belonging to the LIM domain protein family. The final set of 20 energy-refined NMR conformers has an average rmsd relative to the mean structure of 0.55 A for the backbone atoms of residues 3-30. Calculations without zinc atom constraints unambiguously identified Cys 5, Cys 8, His 26, and Cys 29 as the zinc-coordinating residues. LIM domains consist of two sequential zinc-binding modules and the NMR structure of the ZF-1-zinc complex is the first example of a structure of an isolated module. Comparison with the known structures of the N-terminal zinc-binding modules of both the second LIM domain of chicken CRP and rat CRIP with which ZF-1 shares 50% and 43% sequence identity, respectively, supports the notion that the zinc-binding modules of the LIM domain have a conserved structural motif and identifies local regions of structural diversity. The similarities include conserved zinc-coordinating residues, a rubredoxin knuckle involving Cys 5 and Cys 8, and the coordination of the zinc ion by histidine N delta in contrast to the more usual coordination by N epsilon observed for other zinc-finger domains. The present structure determination of the ZF-1-zinc complex establishes the N-terminal half of a LIM domain as an independent folding unit. The structural similarities of N- and C-terminal zinc-binding modules of the LIM domains, despite limited sequence identity, lead to the proposal of a single zinc-binding motif in LIM domains. The coordinates are available from the Brookhaven protein data bank, entry 1ZFO.

PubMed: 8841116
DOI: 10.1021/bi961149j

Experimental method

SOLUTION NMR