PDBsum entry 1bbo

DNA binding protein

PDB id: 1bbo

Contents

Protein chain

57 a.a. *

Metals

_ZN ×2

* Residue conservation analysis

PDB id:

1bbo

Name:

DNA binding protein

Title:

High-resolution solution structure of the double cys2 His2 zinc finger from the human enhancer binding protein mbp-1

Structure:

Human enhancer-binding protein mbp-1. Chain: a. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606

NMR struc:

60 models

Authors:

G.M.Clore,J.G.Omichinski,A.M.Gronenborn

Key ref:

J.G.Omichinski et al. (1992). High-resolution solution structure of the double Cys2His2 zinc finger from the human enhancer binding protein MBP-1. Biochemistry, 31, 3907-3917. PubMed id: 1567844 DOI: 10.1021/bi00131a004

Date:

01-May-92 Release date: 31-Oct-93

Protein chain

P15822  (ZEP1_HUMAN) -  Zinc finger protein 40 from Homo sapiens

Seq: 2718 a.a.

Struc: 57 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1021/bi00131a004

Biochemistry 31:3907-3917 (1992)

PubMed id: 1567844

High-resolution solution structure of the double Cys2His2 zinc finger from the human enhancer binding protein MBP-1.

J.G.Omichinski, G.M.Clore, M.Robien, K.Sakaguchi, E.Appella, A.M.Gronenborn.

ABSTRACT

The high-resolution three-dimensional structure of a synthetic 57-residue peptide comprising the double zinc finger of the human enhancer binding protein MBP-1 has been determined in solution by nuclear magnetic resonance spectroscopy on the basis of 1280 experimental restraints. A total of 30 simulated annealing structures were calculated. The backbone atomic root-mean-square distributions about the mean coordinate positions are 0.32 and 0.33 A for the N- and C-terminal fingers, respectively, and the corresponding values for all atoms, excluding disordered surface side chains, are 0.36 and 0.40 A. Each finger comprises an irregular antiparallel sheet and a helix, with the zinc tetrahedrally coordinated to two cysteines and two histidines. The overall structure is nonglobular in nature, and the angle between the long axes of the helices is 47 +/- 5 degrees. The long axis of the antiparallel sheet in the N-terminal finger is approximately parallel to that of the helix in the C-terminal finger. Comparison of this structure with the X-ray structure of the Zif-268 triple finger complexed with DNA indicates that the relative orientation of the individual zinc fingers is clearly distinct in the two cases. This difference can be attributed to the presence of a long Lys side chain in the C-terminal finger of MBP-1 at position 40, instead of a short Ala or Ser side chain at the equivalent position in Zif-268. This finding suggests that different contacts may be involved in the binding of the zinc fingers of MBP-1 and Zif-268 to DNA, consistent with the findings from methylation interference experiments that the two fingers of MBP-1 contact 10 base pairs, while the three fingers of Zif-268 contact only 9 base pairs.