6csl | pdb_00006csl

Pneumococcal PhtD protein 269-339 fragment with bound Zn(II)

spinqualitylabelsall models 6csl, resolution 1.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6csl is a 1 chain structure with sequence from "diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Gene: phtD ("Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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