1ACP

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

Summary for 1ACP

• Entry DOI: 10.2210/pdb1acp/pdb
• Descriptor: ACYL-CARRIER PROTEIN (1 entity in total)
• Functional Keywords: fatty acid synthesis protein
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A6A8
• Total number of polymer chains: 1
• Total formula weight: 8514.26

Authors

Prestegard, J.H.,Kim, Y. (deposition date: 1990-07-29, release date: 1993-04-15, Last modification date: 2024-04-10)

Primary citation

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

Experimental method

SOLUTION NMR