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2PNE

Crystal Structure of the Snow Flea Antifreeze Protein

Summary for 2PNE
Entry DOI10.2210/pdb2pne/pdb
Descriptor6.5 kDa glycine-rich antifreeze protein (2 entities in total)
Functional Keywordsantifreeze protein, chemical protein synthesis, native chemical ligation
Biological sourceHypogastrura harveyi (snow flea)
Total number of polymer chains1
Total formula weight6489.81
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 citationPentelute, 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: 18598029
DOI: 10.1021/ja8013538
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (0.98 Å)
Structure validation

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