GntR-like bacterial transcription factors

Protein family

Bacterial regulatory proteins, gntR family

solution structure of streptmycal repressor trar

Identifiers
Symbol| GntR
Pfam| PF00392
Pfam clan| CL0123
InterPro| IPR000524
PROSITE| PDOC00042
SCOP2| 1e2x / SCOPe / SUPFAM
| Available protein structures:

Pfam | structures / ECOD
PDB| RCSB PDB; PDBe; PDBj
PDBsum| structure summary

In molecular biology, the GntR-like bacterial transcription factors are a family of transcription factors.

## Background

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Many bacterial transcription regulation proteins bind DNA through a helix-turn-helix (HTH) motif, which can be classified into subfamilies on the basis of sequence similarities. The HTH GntR family has many members distributed among diverse bacterial groups that regulate various biological processes. It was named GntR after the Bacillus subtilis repressor of the gluconate operon.[1] Family members include GntR, HutC, KorA, NtaR, FadR, ExuR, FarR, DgoR, PhnF and PlmA.[2]

The crystal structure of the FadR protein has been determined.[3] In general, these proteins contain a DNA-binding HTH domain at the N-terminus, and an effector-binding or oligomerisation domain at the C-terminus. The DNA-binding domain is well conserved in structure for the whole of the GntR family, consisting of a 3-helical bundle core with a small beta-sheet (wing); the GntR winged helix structure is similar to that found in several other transcriptional regulator families. The regions outside the DNA-binding domain are more variable and are consequently used to define GntR subfamilies.[4]

## References

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1. ^ Haydon DJ, Guest JR (April 1991). "A new family of bacterial regulatory proteins". FEMS Microbiol. Lett. 63 (2–3): 291–295\. doi:10.1016/0378-1097(91)90101-f. PMID 2060763.2–3&rft.pages=291-295&rft.date=1991-04&rft_id=info:doi/10.1016/0378-1097(91)90101-f&rft_id=info:pmid/2060763&rft.aulast=Haydon&rft.aufirst=DJ&rft.au=Guest,+JR&rft_id=https://doi.org/10.1016%2F0378-1097%2891%2990101-f&rfr_id=info:sid/en.wikipedia.org:GntR-like+bacterial+transcription+factors" class="Z3988">
2. ^ Lee, Martin H.; Scherer, Michael; Rigali, Sébastien; Golden, James W. (2003-08-01). "PlmA, a new member of the GntR family, has plasmid maintenance functions in Anabaena sp. strain PCC 7120". Journal of Bacteriology. 185 (15): 4315–4325\. doi:10.1128/jb.185.15.4315-4325.2003. ISSN 0021-9193. PMC 165748. PMID 12867439.4315-4325&rft.date=2003-08-01&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC165748#id-name=PMC&rft.issn=0021-9193&rft_id=info:pmid/12867439&rft_id=info:doi/10.1128/jb.185.15.4315-4325.2003&rft.aulast=Lee&rft.aufirst=Martin+H.&rft.au=Scherer,+Michael&rft.au=Rigali,+Sébastien&rft.au=Golden,+James+W.&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC165748&rfr_id=info:sid/en.wikipedia.org:GntR-like+bacterial+transcription+factors" class="Z3988">
3. ^ van Aalten DM, DiRusso CC, Knudsen J, Wierenga RK (October 2000). "Crystal structure of FadR, a fatty acid-responsive transcription factor with a novel acyl coenzyme A-binding fold". EMBO J. 19 (19): 5167–77\. doi:10.1093/emboj/19.19.5167. PMC 302096. PMID 11013219.5167-77&rft.date=2000-10&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC302096#id-name=PMC&rft_id=info:pmid/11013219&rft_id=info:doi/10.1093/emboj/19.19.5167&rft.aulast=van+Aalten&rft.aufirst=DM&rft.au=DiRusso,+CC&rft.au=Knudsen,+J&rft.au=Wierenga,+RK&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC302096&rfr_id=info:sid/en.wikipedia.org:GntR-like+bacterial+transcription+factors" class="Z3988">
4. ^ Rigali S, Derouaux A, Giannotta F, Dusart J (April 2002). "Subdivision of the helix-turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR, and YtrA subfamilies". J. Biol. Chem. 277 (15): 12507–12515\. doi:10.1074/jbc.M110968200. PMID 11756427.12507-12515&rft.date=2002-04&rft_id=info:doi/10.1074/jbc.M110968200&rft_id=info:pmid/11756427&rft.aulast=Rigali&rft.aufirst=S&rft.au=Derouaux,+A&rft.au=Giannotta,+F&rft.au=Dusart,+J&rft_id=https://doi.org/10.1074%2Fjbc.M110968200&rfr_id=info:sid/en.wikipedia.org:GntR-like+bacterial+transcription+factors" class="Z3988">

This article incorporates text from the public domain Pfam and InterPro: IPR000524