1m1g: Difference between revisions

Revision as of 23:00, 2 July 2008

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File:1m1g.png

Template:STRUCTURE 1m1g

Crystal Structure of Aquifex aeolicus N-utilization substance G (NusG), Space Group P2(1)Crystal Structure of Aquifex aeolicus N-utilization substance G (NusG), Space Group P2(1)

Template:ABSTRACT PUBMED 12198166

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of Aquifex aeolicus N-utilization substance G (NusG), Space Group P2(1)'''
+===Crystal Structure of Aquifex aeolicus N-utilization substance G (NusG), Space Group P2(1)===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12198166}}, adds the Publication Abstract to the page
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 [[Category: Rnp motif]]
 [[Category: Transcription termination]]
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