3EWG

Crystal structure of the N-terminal domain of NusG (NGN) from Methanocaldococcus jannaschii

Summary for 3EWG

• Entry DOI: 10.2210/pdb3ewg/pdb
• Descriptor: Putative transcription antitermination protein nusG, 1,4-DIETHYLENE DIOXIDE (3 entities in total)
• Functional Keywords: alpha/beta structure, antiparallel beta sheet, flanked alpha helices, transcription
• Biological source: Methanocaldococcus jannaschii (Methanococcus jannaschii)
• Total number of polymer chains: 1
• Total formula weight: 10329.98

Authors

Zhou, H.H.,Liu, Q.,Gao, Y.X.,Teng, M.K.,Niu, L.W. (deposition date: 2008-10-15, release date: 2009-06-16, Last modification date: 2023-11-01)

Primary citation

Zhou, H.H.,Liu, Q.,Gao, Y.X.,Teng, M.K.,Niu, L.W.
Crystal structure of NusG N-terminal (NGN) domain from Methanocaldococcus jannaschii and its interaction with rpoE''
Proteins, 76:787-793, 2009

PubMed Abstract: Transcription in archaea employs a eukaryotic-type transcription apparatus but uses bacterial-type transcription factors. NusG is one of the few archaeal transcription factors whose orthologs are essential in both bacteria and eukaryotes. Archaeal NusG is composed of only an NusG N-terminal (NGN) domain and a KOW domain, which is similar to bacterial NusG but not to the eukaryotic ortholog, Spt5. However, archaeal NusG was confirmed recently to form a complex with rpoE'' that was similar to the Spt5-Spt4 complex. Thus, archaeal NusG presents hybrid features of Spt5 and bacterial NusG. Here we report the crystal structure of NGN from the archaea Methanocaldococcus jannaschii (MjNGN). MjNGN folds to an alpha-beta-alpha sandwich without the appendant domain of bacterial NGNs, and forms a unique homodimer in crystal and solution. MjNGN alone was found to be sufficient for rpoE'' binding and an MjNGN-rpoE'' model has been constructed by rigid docking.

PubMed: 19475703
DOI: 10.1002/prot.22465

Experimental method

X-RAY DIFFRACTION (2.04 Å)