Permease of phosphotransferase system

In today's world, Permease of phosphotransferase system is a topic that has captured everyone's attention, whether due to its historical relevance, its impact on modern society or its influence on the development of technology. For centuries, Permease of phosphotransferase system has been the subject of study, debate and controversy, and its importance continues to increase. In this article, we will explore the various facets of Permease of phosphotransferase system, from its origins to its influence today, considering its impact on different areas of daily life. We will also examine the opinions and perspectives of experts in the field, with the goal of offering a broad and comprehensive overview of this fascinating topic.

Phosphotransferase permease
Identifiers
SymbolPTS
PfamPF03611
InterProIPR004703
TCDB4.A.7
OPM superfamily426
OPM protein5zov
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Permease of phosphotransferase system (or PTS-AG superfamily according to TCDB) is a superfamily of phosphotransferase enzymes that facilitate the transport of L-ascorbate (A) and galactitol (G). Classification has been established through phylogenic analysis and bioinformatics.[1][2]

The bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) transports and phosphorylates its sugar substrates in a single energy-coupled step. This transport process is dependent on several cytoplasmic phosphoryl transfer proteins - Enzyme I (I), HPr, Enzyme IIA (IIA), and Enzyme IIB (IIB)) as well as the integral membrane sugar permease (IIC).[3][4] The PTS Enzyme II complexes are derived from independently evolving 4 PTS Enzyme II complex superfamilies, that include the (1) Glucose (Glc),(2) Mannose (Man), (3) Ascorbate-Galactitol (Asc-Gat) and (4) Dihydroxyacetone (Dha) superfamilies.

The four families that make up the PTS-GFL superfamily include:

See also

References

  1. ^ Chen JS, Reddy V, Chen JH, Shlykov MA, Zheng WH, Cho J, Yen MR, Saier MH (2012-01-01). "Phylogenetic characterization of transport protein superfamilies: superiority of SuperfamilyTree programs over those based on multiple alignments". Journal of Molecular Microbiology and Biotechnology. 21 (3–4): 83–96. doi:10.1159/000334611. PMC 3290041. PMID 22286036.
  2. ^ Nguyen TX, Yen MR, Barabote RD, Saier MH (2006-01-01). "Topological predictions for integral membrane permeases of the phosphoenolpyruvate:sugar phosphotransferase system". Journal of Molecular Microbiology and Biotechnology. 11 (6): 345–60. doi:10.1159/000095636. PMID 17114898.
  3. ^ Luo P, Yu X, Wang W, Fan S, Li X, Wang J (March 2015). "Crystal structure of a phosphorylation-coupled vitamin C transporter". Nature Structural & Molecular Biology. 22 (3): 238–41. doi:10.1038/nsmb.2975. PMID 25686089.
  4. ^ Luo P, Dai S, Zeng J, Duan J, Shi H, Wang J (2018). "Inward-facing conformation of l-ascorbate transporter suggests an elevator mechanism". Cell Discovery. 4: 35. doi:10.1038/s41421-018-0037-y. PMC 6048161. PMID 30038796.

Further reading