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. Author manuscript; available in PMC: 2009 Aug 1.
Published in final edited form as: Structure. 2008 Aug 6;16(8):1183–1194. doi: 10.1016/j.str.2008.05.011

Figure 1. NMR solution and X-ray structures of wild type and mutant CV-N.

Figure 1

(A) Ribbon representations of the monomeric solution structure of wild type CV-N [PDB accession code 2EZM] and the crystal structure of the domain-swapped dimer [PDB accession code 3EZM]. Residue positions changed by mutagenesis in CVNmutDB are indicated by blue spheres. The different polypeptide chains in the domain-swapped dimer are colored green and pink. N- and C-termini of the chains are marked by N and C, respectively and the pseudo-symmetric domains are labeled AM and BM in the monomer and AD, BD, A’D and B’D in the domain-swapped dimer. (B) Amino acid sequences of [P51G]CV-N and CVNmutDB. Residues belonging to domains A and B are labeled green and pink, respectively. Disulfide bonds are indicated by brackets and residues involved in protein-carbohydrate interactions are underlined in the [P51G]CV-N sequence. Identical amino acids in the aligned sequence repeats are marked by dots. Residues that were mutated in CVNmutDB are colored blue. (C) Ribbon superposition of the NMR solution structures of CVNmutDB (green) and wild type CV-N (pink).