1.2 Angstroms crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold

Research output: Contribution to journal › Article › peer-review

Standard

1.2 Angstroms crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold. / Riboldi-Tunnicliffe, A; Isaacs, N W; Mitchell, T J.

In: FEBS Letters, Vol. 579, No. 24, 10.10.2005, p. 5353-60.

Research output: Contribution to journal › Article › peer-review

Harvard

Riboldi-Tunnicliffe, A, Isaacs, NW & Mitchell, TJ 2005, '1.2 Angstroms crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold', FEBS Letters, vol. 579, no. 24, pp. 5353-60. https://doi.org/10.1016/j.febslet.2005.08.066

APA

Riboldi-Tunnicliffe, A., Isaacs, N. W., & Mitchell, T. J. (2005). 1.2 Angstroms crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold. FEBS Letters, 579(24), 5353-60. https://doi.org/10.1016/j.febslet.2005.08.066

Vancouver

Riboldi-Tunnicliffe A, Isaacs NW, Mitchell TJ. 1.2 Angstroms crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold. FEBS Letters. 2005 Oct 10;579(24):5353-60. https://doi.org/10.1016/j.febslet.2005.08.066

Author

Riboldi-Tunnicliffe, A ; Isaacs, N W ; Mitchell, T J. / 1.2 Angstroms crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold. In: FEBS Letters. 2005 ; Vol. 579, No. 24. pp. 5353-60.

Bibtex

@article{4eb10a091672417f9b13c534d0061e03,
title = "1.2 Angstroms crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold",
abstract = "The recently described pneumococcal histidine triad protein family has been shown to be highly conserved within the pneumococcus. As part of our structural genomics effort on proteins from Streptococcus pneumoniae, we have expressed, crystallised and solved the structure of PhtA-166-220 at 1.2 Angstroms using remote SAD with zinc. The structure of PhtA-166-220 shows no similarity to any protein structure. The overall fold contains 3beta-strands and a single short alpha-helix. The structure appears to contain a novel zinc binding motif. The remaining 4 histidine triad repeats from PhtA have been modelled based on the crystal structure of the PhtA histidine triad repeat 2. From this modelling work, we speculate that only three of the five histidine triad repeats contain the residues in the correct geometry to allow the binding of a zinc ion.",
keywords = "Amino Acid Sequence, Bacterial Proteins, Binding Sites, Crystallography, X-Ray, Histidine, Models, Molecular, Molecular Sequence Data, Protein Conformation, Streptococcus pneumoniae, Zinc",
author = "A Riboldi-Tunnicliffe and Isaacs, {N W} and Mitchell, {T J}",
year = "2005",
month = oct,
day = "10",
doi = "10.1016/j.febslet.2005.08.066",
language = "English",
volume = "579",
pages = "5353--60",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "24",

}

RIS

TY - JOUR

T1 - 1.2 Angstroms crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold

AU - Riboldi-Tunnicliffe, A

AU - Isaacs, N W

AU - Mitchell, T J

PY - 2005/10/10

Y1 - 2005/10/10

N2 - The recently described pneumococcal histidine triad protein family has been shown to be highly conserved within the pneumococcus. As part of our structural genomics effort on proteins from Streptococcus pneumoniae, we have expressed, crystallised and solved the structure of PhtA-166-220 at 1.2 Angstroms using remote SAD with zinc. The structure of PhtA-166-220 shows no similarity to any protein structure. The overall fold contains 3beta-strands and a single short alpha-helix. The structure appears to contain a novel zinc binding motif. The remaining 4 histidine triad repeats from PhtA have been modelled based on the crystal structure of the PhtA histidine triad repeat 2. From this modelling work, we speculate that only three of the five histidine triad repeats contain the residues in the correct geometry to allow the binding of a zinc ion.

AB - The recently described pneumococcal histidine triad protein family has been shown to be highly conserved within the pneumococcus. As part of our structural genomics effort on proteins from Streptococcus pneumoniae, we have expressed, crystallised and solved the structure of PhtA-166-220 at 1.2 Angstroms using remote SAD with zinc. The structure of PhtA-166-220 shows no similarity to any protein structure. The overall fold contains 3beta-strands and a single short alpha-helix. The structure appears to contain a novel zinc binding motif. The remaining 4 histidine triad repeats from PhtA have been modelled based on the crystal structure of the PhtA histidine triad repeat 2. From this modelling work, we speculate that only three of the five histidine triad repeats contain the residues in the correct geometry to allow the binding of a zinc ion.

KW - Amino Acid Sequence

KW - Bacterial Proteins

KW - Binding Sites

KW - Crystallography, X-Ray

KW - Histidine

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Protein Conformation

KW - Streptococcus pneumoniae

KW - Zinc

U2 - 10.1016/j.febslet.2005.08.066

DO - 10.1016/j.febslet.2005.08.066

M3 - Article

C2 - 16194532

VL - 579

SP - 5353

EP - 5360

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 24

ER -