4IWM

Crystal Structure of the Conserved Hypothetical Protein MJ0927 from Methanocaldococcus jannaschii (in P21 form)

Summary for 4IWM

• Entry DOI: 10.2210/pdb4iwm/pdb
• Related: 4IWG
• Descriptor: UPF0135 protein MJ0927 (2 entities in total)
• Functional Keywords: nif3-like, unknown function
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 6
• Total formula weight: 171387.22

Authors

Kuan, S.M.,Chen, S.C.,Yang, C.S.,Chen, Y.R.,Liu, Y.H.,Chen, Y. (deposition date: 2013-01-24, release date: 2014-01-29, Last modification date: 2021-04-21)

Primary citation

Chen, S.C.,Huang, C.H.,Yang, C.S.,Kuan, S.M.,Lin, C.T.,Chou, S.H.,Chen, Y.
Crystal structure of a conserved hypothetical protein MJ0927 from Methanocaldococcus jannaschii reveals a novel quaternary assembly in the Nif3 family.
Biomed Res Int, 2014:171263-171263, 2014

PubMed Abstract: A Nif3 family protein of Methanocaldococcus jannaschii, MJ0927, is highly conserved from bacteria to humans. Although several structures of bacterial Nif3 proteins are known, no structure representing archaeal Nif3 has yet been reported. The crystal structure of Methanocaldococcus jannaschii MJ0927 was determined at 2.47 Å resolution to understand the structural differences between the bacterial and archaeal Nif3 proteins. Intriguingly, MJ0927 is found to adopt an unusual assembly comprising a trimer of dimers that forms a cage-like architecture. Electrophoretic mobility-shift assays indicate that MJ0927 binds to both single-stranded and double-stranded DNA. Structural analysis of MJ0927 reveals a positively charged region that can potentially explain its DNA-binding capability. Taken together, these data suggest that MJ0927 adopts a novel quartenary architecture that could play various DNA-binding roles in Methanocaldococcus jannaschii.

PubMed: 25243119
DOI: 10.1155/2014/171263

Experimental method

X-RAY DIFFRACTION (2.7 Å)