1BDW

GRAMICIDIN D FROM BACILLUS BREVIS (ACTIVE FORM)

Summary for 1BDW

• Entry DOI: 10.2210/pdb1bdw/pdb
• Related: 1AL4 1ALX 1ALZ 1AV2 1C4D 1GMK 1GRM 1JNO 1JO3 1JO4 1KQE 1MAG 1MIC 1NG8 1NRM 1NRU 1NT5 1NT6 1TK2 1TKQ 1W5U 2IZQ 2XDC 3L8L
• Related PRD ID: PRD_000150
• Descriptor: GRAMICIDIN A, ACETIC ACID (3 entities in total)
• Functional Keywords: gramicidin, antifungal, antibacterial, antibiotic, membrane ion channel, linear gramicidin, double helix
• Biological source: BREVIBACILLUS BREVIS
• Total number of polymer chains: 2
• Total formula weight: 4064.85

Authors

Burkhart, B.M.,Pangborn, W.A.,Duax, W.L. (deposition date: 1998-05-11, release date: 1998-10-14, Last modification date: 2024-10-30)

Primary citation

Burkhart, B.M.,Li, N.,Langs, D.A.,Pangborn, W.A.,Duax, W.L.
The Conducting Form of Gramicidin a is a Right-Handed Double-Stranded Double Helix.
Proc.Natl.Acad.Sci.USA, 95:12950-, 1998

PubMed Abstract: The linear pentadecapeptide antibiotic, gramicidin D, is a naturally occurring product of Bacillus brevis known to form ion channels in synthetic and natural membranes. The x-ray crystal structures of the right-handed double-stranded double-helical dimers (DSDH) reported here agree with 15N-NMR and CD data on the functional gramicidin D channel in lipid bilayers. These structures demonstrate single-file ion transfer through the channels. The results also indicate that previous crystal structure reports of a left-handed double-stranded double-helical dimer in complex with Cs+ and K+ salts may be in error and that our evidence points to the DSDH as the major conformer responsible for ion transport in membranes.

PubMed: 9789021
DOI: 10.1073/PNAS.95.22.12950

Experimental method

X-RAY DIFFRACTION (1.7 Å)