6l6g

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Crystal structure of SeMet_Lpg0189Crystal structure of SeMet_Lpg0189

Structural highlights

6l6g is a 2 chain structure with sequence from Legionella pneumophila subsp. pneumophila str. Philadelphia 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.98Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q5ZZ22_LEGPH

Publication Abstract from PubMed

Lpg0189 is a type II secretion system-dependent extracellular protein with unknown function from Legionella pneumophila. Herein, we determined the crystal structure of Lpg0189 at 1.98A resolution by using single-wavelength anomalous diffraction (SAD). Lpg0189 folds into a novel chair-shaped architecture, with two sheets roughly perpendicular to each other. Bioinformatics analysis suggests Lpg0189 and its homologues are unique to Legionellales and evolved divergently. The interlinking structural and bioinformatics studies provide a better understanding of this hypothetical protein.

Crystal structure of a hypothetical T2SS effector Lpg0189 from Legionella pneumophila reveals a novel protein fold.,Chen X, Liu S, Jiang S, Zhang X, Zhang N, Ma J, Ge H Biochem Biophys Res Commun. 2019 Nov 6. pii: S0006-291X(19)32111-4. doi:, 10.1016/j.bbrc.2019.10.195. PMID:31706575[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Chen X, Liu S, Jiang S, Zhang X, Zhang N, Ma J, Ge H. Crystal structure of a hypothetical T2SS effector Lpg0189 from Legionella pneumophila reveals a novel protein fold. Biochem Biophys Res Commun. 2019 Nov 6. pii: S0006-291X(19)32111-4. doi:, 10.1016/j.bbrc.2019.10.195. PMID:31706575 doi:http://dx.doi.org/10.1016/j.bbrc.2019.10.195

6l6g, resolution 1.98Å

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OCA