1Z2F

solution structure of CfAFP-501

Summary for 1Z2F

• Entry DOI: 10.2210/pdb1z2f/pdb
• NMR Information: BMRB: 6111
• Descriptor: Antifreeze Protein Isoform 501 (1 entity in total)
• Functional Keywords: antifreeze protein, choristoneura fumiferana, spruce budworm, solution structure
• Biological source: Choristoneura fumiferana (spruce budworm)
• Total number of polymer chains: 1
• Total formula weight: 12546.90

Authors

Li, C.,Jin, C. (deposition date: 2005-03-08, release date: 2005-10-11, Last modification date: 2024-10-23)

Primary citation

Li, C.,Guo, X.,Jia, Z.,Xia, B.,Jin, C.
Solution Structure of an Antifreeze Protein CfAFP-501 from Choristoneura fumiferana
J.Biomol.Nmr, 32:251-256, 2005

PubMed Abstract: Antifreeze proteins (AFPs) are widely employed by various organisms as part of their overwintering survival strategy. AFPs have the unique ability to suppress the freezing point of aqueous solution and inhibit ice recrystallization through binding to the ice seed crystals and restricting their growth. The solution structure of CfAFP-501 from spruce budworm has been determined by NMR spectroscopy. Our result demonstrates that CfAFP-501 retains its rigid and highly regular structure in solution. Overall, the solution structure is similar to the crystal structure except the N- and C-terminal regions. NMR spin-relaxation experiments further indicate the overall rigidity of the protein and identify a collection of residues with greater flexibilities. Furthermore, Pro91 shows a cis conformation in solution instead of the trans conformation determined in the crystal structure.

PubMed: 16132825
DOI: 10.1007/s10858-005-8206-3

Experimental method

SOLUTION NMR