3ZFJ

N-terminal domain of pneumococcal PhtD protein with bound Zn(II)

3ZFJ の概要

• エントリーDOI: 10.2210/pdb3zfj/pdb
• NMR情報: BMRB: 18943
• 分子名称: PNEUMOCOCCAL HISTIDINE TRIAD PROTEIN D, ZINC ION (2 entities in total)
• 機能のキーワード: zinc-binding protein, zinc transfer
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15847.83

構造登録者

Bersch, B.,Bougault, C.,Favier, A.,Gabel, F.,Roux, L.,Vernet, T.,Durmort, C. (登録日: 2012-12-11, 公開日: 2013-11-20, 最終更新日: 2024-06-19)

主引用文献

Bersch, B.,Bougault, C.,Roux, L.,Favier, A.,Vernet, T.,Durmort, C.
New Insights Into Histidine Triad Proteins: Solution Structure of a Streptococcus Pneumoniae Phtd Domain and Zinc Transfer to Adcaii.
Plos One, 8:81168-, 2013

PubMed Abstract: Zinc (Zn(2+)) homeostasis is critical for pathogen host colonization and invasion. Polyhistidine triad (Pht) proteins, located at the surface of various streptococci, have been proposed to be involved in Zn(2+) homeostasis. The phtD gene, coding for a Zn(2+)-binding protein, is organized in an operon with adcAII coding for the extracellular part of a Zn(2+) transporter. In the present work, we investigate the relationship between PhtD and AdcAII using biochemical and structural biology approaches. Immuno-precipitation experiments on purified membranes of Streptococcus pneumoniae (S. pneumoniae) demonstrate that native PhtD and AdcAII interact in vivo confirming our previous in vitro observations. NMR was used to demonstrate Zn(2+) transfer from the Zn(2+)-bound form of a 137 amino acid N-terminal domain of PhtD (t-PhtD) to AdcAII. The high resolution NMR structure of t-PhtD shows that Zn(2+) is bound in a tetrahedral site by histidines 83, 86, and 88 as well as by glutamate 63. Comparison of the NMR parameters measured for apo- and Zn(2+)-t-PhtD shows that the loss of Zn(2+) leads to a diminished helical propensity at the C-terminus and increases the local dynamics and overall molecular volume. Structural comparison with the crystal structure of a 55-long fragment of PhtA suggests that Pht proteins are built from short repetitive units formed by three β-strands containing the conserved HxxHxH motif. Taken together, these results support a role for S. pneumoniae PhtD as a Zn(2+) scavenger for later release to the surface transporter AdcAII, leading to Zn(2+) uptake.

PubMed: 24312273
DOI: 10.1371/JOURNAL.PONE.0081168

実験手法

SOLUTION NMR