1ACP

REFINEMENT OF THE NMR STRUCTURES FOR ACYL CARRIER PROTEIN WITH SCALAR COUPLING DATA

1ACP の概要

• エントリーDOI: 10.2210/pdb1acp/pdb
• 分子名称: ACYL-CARRIER PROTEIN (1 entity in total)
• 機能のキーワード: fatty acid synthesis protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A6A8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8514.26

構造登録者

Prestegard, J.H.,Kim, Y. (登録日: 1990-07-29, 公開日: 1993-04-15, 最終更新日: 2024-04-10)

主引用文献

Kim, Y.,Prestegard, J.H.
Refinement of the NMR structures for acyl carrier protein with scalar coupling data.
Proteins, 8:377-385, 1990

PubMed Abstract: Structure determination of small proteins using NMR data is most commonly pursued by combining NOE derived distance constraints with inherent constraints based on chemical bonding. Ideally, one would make use of a variety of experimental observations, not just distance constraints. Here, coupling constant constraints have been added to molecular mechanics and molecular dynamics protocols for structure determination in the form of a psuedoenergy function that is minimized in a search for an optimum molecular conformation. Application is made to refinement of a structure for a 77 amino acid protein involved in fatty acid synthesis, Escherichia coli acyl carrier protein (ACP). 54 3JHN alpha coupling constants, 12 coupling constants for stereospecifically assigned side chain protons, and 450 NOE distance constraints were used to calculate the 3-D structure of ACP. A three-step protocol for a molecular dynamics calculation is described, in analogy to the protocol previously used in molecular mechanics calculations. The structures calculated with the molecular mechanics approach and the molecular dynamics approach using a rigid model for the protein show similar molecular energies and similar agreement with experimental distance and coupling constant constraints. The molecular dynamics approach shows some advantage in overcoming local minimum problems, but only when a two-state averaging model for the protein was used, did molecular energies drop significantly.

PubMed: 2091027
DOI: 10.1002/prot.340080411

実験手法

SOLUTION NMR