1MAG

GRAMICIDIN A IN HYDRATED DMPC BILAYERS, SOLID STATE NMR

1MAG の概要

• エントリーDOI: 10.2210/pdb1mag/pdb
• 関連するPDBエントリー: 1AL4 1ALX 1ALZ 1AV2 1BDW 1C4D 1GMK 1GRM 1JNO 1JO3 1JO4 1KQE 1MIC 1NG8 1NRM 1NRU 1NT5 1NT6 1TK2 1TKQ 1W5U 2IZQ 2XDC 3L8L
• 関連するBIRD辞書のPRD_ID: PRD_000150
• 分子名称: GRAMICIDIN A (1 entity in total)
• 機能のキーワード: gramicidin, antifungal, antibacterial, antibiotic, membrane ion channel, linear gramicidin, oriented bilayers
• 由来する生物種: BREVIBACILLUS BREVIS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 3764.59

構造登録者

Ketchem, R.R.,Roux, B.,Cross, T.A. (登録日: 1996-06-06, 公開日: 1997-01-11, 最終更新日: 2024-10-16)

主引用文献

Ketchem, R.R.,Lee, K.C.,Huo, S.,Cross, T.A.
Macromolecular Structural Elucidation with Solid-State NMR-Derived Orientational Constraints.
J.Biomol.NMR, 8:1-, 1996

PubMed Abstract: The complete structure determination of a polypeptide in a lipid bilayer environment is demonstrated built solely upon orientational constraints derived from solid-state NMR observations. Such constraints are obtained from isotopically labeled samples uniformly aligned with respect to the B(0) field. Each observation constrains the molecular frame with respect to B(0) and the bilayer normal, which are arranged to be parallel. These constraints are not only very precise ( a few tenths of a degree), but also very accurate. This is clearly demonstrated as the backbone structure is assembled sequentially and the i to i + 6 hydrogen bonds in this structure of the gramicidin channel are shown on average to be within 0.5 A of ideal geometry. Similarly, the side chains are assembled independently and in a radial direction from the backbone. The lack of considerable atomic overlap between side chains also demonstrates the accuracy of the constraints. Through this complete structure, solid-state NMR is demonstrated as an approach for determining three-dimensional macromolecular structure.

PubMed: 8810522
DOI: 10.1007/BF00198135

実験手法

SOLID-STATE NMR