Structural highlights
Function
Q0PC47_CAMJE
Publication Abstract from PubMed
Bacterial lipoproteins play an important role in bacterial pathogenesis and physiology. The genome of Campylobacter jejuni, a major foodborn pathogen, is predicted to contain over 20 lipoproteins. However, the functions of the majority of C. jejuni lipoproteins remain unknown. The Cj0090 protein is encoded by a lipoprotein operon composed of cj0089, cj0090, and cj0091. Here, we report the crystal structure of Cj0090 at 1.9 A resolution, revealing a novel variant of the immunoglobulin fold with beta-sandwich architecture. The structure suggests that Cj0090 may be involved in protein-protein interactions, consistent with a possible role for bacterial lipoproteins. Proteins 2012;. (c) 2012 Wiley Periodicals, Inc.
Crystal structure of the Campylobacter jejuni Cj0090 protein reveals a novel variant of the immunoglobulin fold among bacterial lipoproteins.,Paek S, Kawai F, Choi KJ, Yeo HJ Proteins. 2012 Dec;80(12):2804-9. doi: 10.1002/prot.24182. Epub 2012 Oct 16. PMID:22987763[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Paek S, Kawai F, Choi KJ, Yeo HJ. Crystal structure of the Campylobacter jejuni Cj0090 protein reveals a novel variant of the immunoglobulin fold among bacterial lipoproteins. Proteins. 2012 Dec;80(12):2804-9. doi: 10.1002/prot.24182. Epub 2012 Oct 16. PMID:22987763 doi:http://dx.doi.org/10.1002/prot.24182