1nz8: Difference between revisions

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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nz8 ConSurf].
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Revision as of 08:28, 8 February 2016

Solution Structure of the N-utilization substance G (NusG) N-terminal (NGN) domain from Thermus thermophilusSolution Structure of the N-utilization substance G (NusG) N-terminal (NGN) domain from Thermus thermophilus

Structural highlights

1nz8 is a 1 chain structure with sequence from "flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:NusG ("Flavobacterium thermophilum" Yoshida and Oshima 1971)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, TOPSAN

Function

[NUSG_THET8] Participates in transcription elongation, termination and antitermination (By similarity).

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 PubMed

NusG is an essential bacterial protein modulator of transcriptional elongation and termination events, and interacts directly with RNA polymerase and Rho protein. Found also in Archaea, NusG shows stretches of sequence similarity to the eukaryotic transcription elongation factor Spt5. Herein, the three-dimensional solution structure of the bacterial NusG from Thermus thermophilus, which shows 43% amino acid sequence similarity to the Escherichia coli NusG, is described, and a survey of NusG and Spt5 amino acid sequences is presented. Although there is a clear evolutionary and functional relationship between these proteins, it is evident from the structural, sequence, and biochemical data that their binding specificities to both nucleic acids and other proteins differ.

Structural and sequence comparisons arising from the solution structure of the transcription elongation factor NusG from Thermus thermophilus.,Reay P, Yamasaki K, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S Proteins. 2004 Jul 1;56(1):40-51. PMID:15162485[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Reay P, Yamasaki K, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S. Structural and sequence comparisons arising from the solution structure of the transcription elongation factor NusG from Thermus thermophilus. Proteins. 2004 Jul 1;56(1):40-51. PMID:15162485 doi:10.1002/prot.20054
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