Structural highlights
Publication Abstract from PubMed
The bacterium Streptococcus pneumoniae (the pneumococcus) is a major human pathogen that requires Zn(2+) for its survival and virulence in the host environment. Polyhistidine triad protein D (PhtD) has a known role in pneumococcal Zn(2+) homeostasis. However, the mechanistic basis of PhtD function remains unclear, partly due to a lack of structural information. Here, we determined the crystal structure of the fragment PhtD(269-339) , containing the third Zn(2+) -binding histidine triad (HT) motif of the protein. Analysis of the structure suggests that Zn(2+) -binding occurs at the surface of the protein and that all five HT motifs in the protein bind Zn(2+) and share similar structures. These new structural insights aid in our understanding of how the Pht proteins facilitate pneumococcal Zn(2+) acquisition. This article is protected by copyright. All rights reserved.
Structural characterisation of the HT3 motif of the polyhistidine triad protein D from Streptococcus pneumoniae.,Luo Z, Pederick VG, Paton JC, McDevitt CA, Kobe B FEBS Lett. 2018 Jun 1. doi: 10.1002/1873-3468.13122. PMID:29856892[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Luo Z, Pederick VG, Paton JC, McDevitt CA, Kobe B. Structural characterisation of the HT3 motif of the polyhistidine triad protein D from Streptococcus pneumoniae. FEBS Lett. 2018 Jun 1. doi: 10.1002/1873-3468.13122. PMID:29856892 doi:http://dx.doi.org/10.1002/1873-3468.13122
