1SPF

THE NMR STRUCTURE OF THE PULMONARY SURFACTANT-ASSOCIATED POLYPEPTIDE SP-C IN AN APOLAR SOLVENT CONTAINS A VALYL-RICH ALPHA-HELIX


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Submitted: 20 

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This is version 1.3 of the entry. See complete history


Literature

The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix.

Johansson, J.Szyperski, T.Curstedt, T.Wuthrich, K.

(1994) Biochemistry 33: 6015-6023

  • DOI: https://doi.org/10.1021/bi00185a042
  • Primary Citation of Related Structures:  
    1SPF

  • PubMed Abstract: 

    The nuclear magnetic resonance (NMR) structure of the pulmonary surfactant-associated lipoplypeptide C (SP-C) was determined in a mixed solvent of C2H3Cl/C2H3OH/ 1 M HCl 32:64:5 (v/v). Sequence-specific 1H NMR assignments and the collection of conformational constraints were achieved with two-dimensional 1H NMR, and the structure was calculated with the distance geometry program DIANA. The root mean square deviations for the well-defined polypeptide segment of residues 9-34 calculated for the 20 best energy-minimized DIANA conformers relative to their mean are 0.5 and 1.3 A for the polypeptide backbone atoms N, C alpha, and C', and for all heavy atoms, respectively. The 35-residue polypeptide chain of SP-C forms an alpha-helix between positions 9 and 34, which includes two segments of seven and four consecutive valyls that are separated by a single leucyl residue. The N-terminal hexapeptide segment, which includes two palmitoylcysteinyls, is flexibly disordered. The length of the alpha-helix is about 37 A, and the helical segment of residues 13-28, which contains exclusively aliphatic residues with branched side chains, is 23-A long and about 10 A in diameter. The alpha-helix is outstandingly regular, with virtually identical chi 1 angles for all valyl residues. The observation of a helical structure of SP-C was rather unexpected, considering that Val is generally underrepresented in alpha-helices, and it provides intriguing novel insights into the structural basis of SP-C functions as well as into general structural aspects of protein-lipid interactions in biological membranes.


  • Organizational Affiliation

    Institut für Molekularbiologie und Biophysik, Eidenössiche Technische Hochshule-Hönggerberg.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PULMONARY SURFACTANT-ASSOCIATED POLYPEPTIDE C35Sus scrofaMutation(s): 0 
UniProt
Find proteins for P15785 (Sus scrofa)
Explore P15785 
Go to UniProtKB:  P15785
Entity Groups  
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UniProt GroupP15785
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Submitted: 20 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1994-12-20
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-02
    Changes: Database references, Derived calculations, Other