Three‐dimensional structure of acyl carrier protein in solution determined by nuclear magnetic resonance and the combined use of dynamical simulated annealing and distance geometry
The solution conformation of acyl carrier protein from Escherichia coli (77 residues) has been determined on the basis of 423 interproton‐distance restraints and 32 hydrogen‐bonding restraints derived from NMR measurements. A total of nine structures were computed using a hybrid approach combining m...
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Published in | European journal of biochemistry Vol. 175; no. 1; pp. 9 - 15 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Oxford, UK
Blackwell Publishing Ltd
15.07.1988
Blackwell |
Subjects | |
Online Access | Get full text |
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Summary: | The solution conformation of acyl carrier protein from Escherichia coli (77 residues) has been determined on the basis of 423 interproton‐distance restraints and 32 hydrogen‐bonding restraints derived from NMR measurements. A total of nine structures were computed using a hybrid approach combining metric matrix distance geometry and dynamic simulated annealing. The polypeptide fold is well defined with an average backbone atomic root‐mean‐square difference of 0.20 ± 0.03 nm between the final nine converged structures and the mean structure obtained by averaging their coordinates. The principal structural motif is composed of three helices: 1 (residues 3–12), 2 (residues 37–47) and 4 (residues 65–75) which line a hydrophobic cavity. Helices 2 and 4 are approximately parallel to each other and anti‐parallel at an angle of ≊ 150° to helix 1. The smaller helix 3 (residues 56–63) is at an angle of ≊ 100° to helix 4. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0014-2956 1432-1033 |
DOI: | 10.1111/j.1432-1033.1988.tb14159.x |