2PNE
Crystal Structure of the Snow Flea Antifreeze Protein
Summary for 2PNE
Entry DOI | 10.2210/pdb2pne/pdb |
Descriptor | 6.5 kDa glycine-rich antifreeze protein (2 entities in total) |
Functional Keywords | antifreeze protein, chemical protein synthesis, native chemical ligation |
Biological source | Hypogastrura harveyi (snow flea) |
Total number of polymer chains | 1 |
Total formula weight | 6489.81 |
Authors | Pentelute, B.L.,Kent, S.B.H.,Gates, Z.P.,Tereshko, V.,Kossiakoff, A.A.,Kurutz, J.,Dashnau, J.,Vaderkooi, J.M. (deposition date: 2007-04-24, release date: 2008-04-29, Last modification date: 2024-10-16) |
Primary citation | Pentelute, B.L.,Gates, Z.P.,Tereshko, V.,Dashnau, J.L.,Vanderkooi, J.M.,Kossiakoff, A.A.,Kent, S.B. X-ray structure of snow flea antifreeze protein determined by racemic crystallization of synthetic protein enantiomers J.Am.Chem.Soc., 130:9695-9701, 2008 Cited by PubMed Abstract: Chemical protein synthesis and racemic protein crystallization were used to determine the X-ray structure of the snow flea antifreeze protein (sfAFP). Crystal formation from a racemic solution containing equal amounts of the chemically synthesized proteins d-sfAFP and l-sfAFP occurred much more readily than for l-sfAFP alone. More facile crystal formation also occurred from a quasi-racemic mixture of d-sfAFP and l-Se-sfAFP, a chemical protein analogue that contains an additional -SeCH2- moiety at one residue and thus differs slightly from the true enantiomer. Multiple wavelength anomalous dispersion (MAD) phasing from quasi-racemate crystals was then used to determine the X-ray structure of the sfAFP protein molecule. The resulting model was used to solve by molecular replacement the X-ray structure of l-sfAFP to a resolution of 0.98 A. The l-sfAFP molecule is made up of six antiparallel left-handed PPII helixes, stacked in two sets of three, to form a compact brick-like structure with one hydrophilic face and one hydrophobic face. This is a novel experimental protein structure and closely resembles a structural model proposed for sfAFP. These results illustrate the utility of total chemical synthesis combined with racemic crystallization and X-ray crystallography for determining the unknown structure of a protein. PubMed: 18598029DOI: 10.1021/ja8013538 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (0.98 Å) |
Structure validation
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