1M24

Trichotoxin_A50E, An Ion Channel-Forming Polypeptide

Summary for 1M24

• Entry DOI: 10.2210/pdb1m24/pdb
• Related: 1AMT 1DLZ 1EE7 1GQ0 1IH9 1JOH 1OB4 1OB6 1OB7 1R9U
• Related PRD ID: PRD_000160
• Descriptor: TRICHOTOXIN_A50E, ACETONITRILE (3 entities in total)
• Functional Keywords: trichotoxin, peptaibol, antibacterial, antifungal, antibiotic
• Biological source: TRICHODERMA VIRIDE
• Total number of polymer chains: 2
• Total formula weight: 3430.18

Authors

Chugh, J.K.,Brueckner, H.,Wallace, B.A. (deposition date: 2002-06-21, release date: 2002-11-06, Last modification date: 2024-04-03)

Primary citation

Chugh, J.K.,Brueckner, H.,Wallace, B.A.
Model for a Helical Bundle Channel Based on the High-Resolution Crystal Structure of Trichotoxin_A50E
Biochemistry, 41:12934-, 2002

PubMed Abstract: Trichotoxin_A50E is an 18-residue peptaibol antibiotic which forms multimeric transmembrane channels through self-association. The crystal structure of trichotoxin has been determined at a resolution of 0.9 A. The trichotoxin sequence contains nine helix-promoting Aib residues, which contribute to the formation of an entirely helical structure that has a central bend of 8-10 degrees located between residues 10-13. Trichotoxin is the first solved structure of the peptaibol family that is all alpha-helix as opposed to containing part or all 3(10)-helix. Gln residues in positions 6 and 17 produce a polar face, and are proposed to form the channel lumen. An octameric model channel has been constructed from the crystal structure. It has a central pore of approximately 4-5 A radius, a size sufficient to enable transport of ions, with a constricted region at one end, formed by a ring of Gln6 residues. Electrostatic calculations are consistent with it being a cationic channel.

PubMed: 12390019
DOI: 10.1021/BI026150Z

Experimental method

X-RAY DIFFRACTION (0.9 Å)