7CAY

Crystal Structure of Lon N-terminal domain protein from Xanthomonas campestris

Summary for 7CAY

• Entry DOI: 10.2210/pdb7cay/pdb
• Descriptor: ATP-dependent protease (1 entity in total)
• Functional Keywords: n-terminal domain, lon protease, protein binding
• Biological source: Xanthomonas campestris pv. campestris
• Total number of polymer chains: 1
• Total formula weight: 21318.29

Authors

Singh, R.,Sharma, B.,Deshmukh, S.,Kumar, A.,Makde, R.D. (deposition date: 2020-06-10, release date: 2020-10-14, Last modification date: 2023-11-29)

Primary citation

Singh, R.,Deshmukh, S.,Kumar, A.,Goyal, V.D.,Makde, R.D.
Crystal structure of XCC3289 from Xanthomonas campestris: homology with the N-terminal substrate-binding domain of Lon peptidase.
Acta Crystallogr.,Sect.F, 76:488-494, 2020

PubMed Abstract: LonA peptidase is a major component of the protein quality-control mechanism in both prokaryotes and the organelles of eukaryotes. Proteins homologous to the N-terminal domain of LonA peptidase, but lacking its other domains, are conserved in several phyla of prokaryotes, including the Xanthomonadales order. However, the function of these homologous proteins (LonNTD-like proteins) is not known. Here, the crystal structure of the LonNTD-like protein from Xanthomonas campestris (XCC3289; UniProt Q8P5P7) is reported at 2.8 Å resolution. The structure was solved by molecular replacement and contains one polypeptide in the asymmetric unit. The structure was refined to an R of 29%. The structure of XCC3289 consists of two domains joined by a long loop. The N-terminal domain (residues 1-112) consists of an α-helix surrounded by β-sheets, whereas the C-terminal domain (residues 123-193) is an α-helical bundle. The fold and spatial orientation of the two domains closely resembles those of the N-terminal domains of the LonA peptidases from Escherichia coli and Mycobacterium avium. The structure is also similar to that of cereblon, a substrate-recognizing component of the E3 ubiquitin ligase complex. The N-terminal domains of both LonA and cereblon are known to be involved in specific protein-protein interactions. This structural analysis suggests that XCC3289 and other LonNTD-like proteins might also be capable of such protein-protein interactions.

PubMed: 33006577
DOI: 10.1107/S2053230X20011875

Experimental method

X-RAY DIFFRACTION (2.8 Å)