1m1g
Crystal Structure of Aquifex aeolicus N-utilization substance G (NusG), Space Group P2(1)
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OverviewOverview
Microbial transcription modulator NusG interacts with RNA polymerase and, termination factor rho, displaying striking functional homology to, eukaryotic Spt5. The protein is also a translational regulator. We have, determined crystal structures of Aquifex aeolicus NusG showing a modular, design: an N-terminal RNP-like domain, a C-terminal element with a KOW, sequence motif and a species-specific immunoglobulin-like fold. The, structures reveal bona fide nucleic acid binding sites, and nucleic acid, binding activities can be detected for NusG from three organisms and for, the KOW element alone. A conserved KOW domain is defined as a new class of, nucleic acid binding folds. This module is a close structural homolog of, tudor protein-protein interaction motifs. Putative protein binding sites, for the RNP and KOW domains can be deduced, which differ from the areas, implicated in nucleic acid interactions. The results strongly argue that, both protein and nucleic acid contacts are important for NusG's functions, and that the factor can act as an adaptor mediating indirect, protein-nucleic acid associations.
About this StructureAbout this Structure
1M1G is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities., Steiner T, Kaiser JT, Marinkovic S, Huber R, Wahl MC, EMBO J. 2002 Sep 2;21(17):4641-53. PMID:12198166
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