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Crystal structure of the N-terminal domain of NusG (NGN) from Methanocaldococcus jannaschiiCrystal structure of the N-terminal domain of NusG (NGN) from Methanocaldococcus jannaschii
Structural highlights
FunctionSPT5_METJA Stimulates transcription elongation.[HAMAP-Rule:MF_00950][1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTranscription 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. Proteins 2009. (c) 2009 Wiley-Liss, Inc. Crystal structure of NusG N-terminal (NGN) domain from Methanocaldococcus jannaschii and its interaction with rpoE,Zhou H, Liu Q, Gao Y, Teng M, Niu L Proteins. 2009 Apr 28. PMID:19475703[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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