3AK0

Crystal Structure of Ancestral Congerin Con-anc'-N28K

Summary for 3AK0

• Entry DOI: 10.2210/pdb3ak0/pdb
• Related: 1c1f 1c1l 1is3 1is4 1is5 1is6 3AJY 3AJZ
• Related PRD ID: PRD_900004
• Descriptor: Ancestral congerin Con-anc, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: ancestral protein, galectin, lectin, sugar binding protein
• Total number of polymer chains: 2
• Total formula weight: 31310.63

Authors

Konno, A.,Kitagawa, A.,Watanabe, M.,Ogawa, T.,Shirai, T. (deposition date: 2010-06-29, release date: 2011-05-18, Last modification date: 2023-11-01)

Primary citation

Konno, A.,Kitagawa, A.,Watanabe, M.,Ogawa, T.,Shirai, T.
Tracing protein evolution through ancestral structures of fish galectin
Structure, 19:711-721, 2011

PubMed Abstract: Ancestral structures of fish galectins (congerins) were determined. The extant isoforms I and II of congerin are the components of a fish biological defense system and have rapidly differentiated under natural selection pressure, by which congerin I has experienced a protein-fold evolution. The dimer structure of the ancestral congerin demonstrated intermediate features of the extant isoforms. The protein-fold evolution was not observed in the ancestral structure, indicating it specifically occurred in congerin I lineage. Details of hydrogen bonding pattern at the dimer interface and the carbohydrate-binding site of the ancestor were different from the current proteins. The differences implied these proteins were under selection pressure for stabilizing dimer structure and differentiation in carbohydrate specificity. The ancestor had rather low cytotoxic activity than offspring, indicating selection was made to enhance this activity of congerins. Combined with functional analyses, the structure revealed atomic details of the differentiation process of the proteins.

PubMed: 21565705
DOI: 10.1016/j.str.2011.02.014

Experimental method

X-RAY DIFFRACTION (1.59 Å)