4iwm
From Proteopedia
Crystal Structure of the Conserved Hypothetical Protein MJ0927 from Methanocaldococcus jannaschii (in P21 form)
Structural highlights
FunctionGCH1L_METJA DNA-binding protein exhibiting the ability to bind to both single-stranded and double-stranded DNA.[1] Publication Abstract from PubMedA 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 A 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. Crystal structure of a conserved hypothetical protein MJ0927 from Methanocaldococcus jannaschii reveals a novel quaternary assembly in the Nif3 family.,Chen SC, Huang CH, Yang CS, Kuan SM, Lin CT, Chou SH, Chen Y Biomed Res Int. 2014;2014:171263. doi: 10.1155/2014/171263. Epub 2014 Aug 28. PMID:25243119[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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