4J4E

Structure of P51G Cyanovirin-N swapped trimer in the P212121 space group

4J4E の概要

• エントリーDOI: 10.2210/pdb4j4e/pdb
• 関連するPDBエントリー: 4J4C 4J4D 4J4F 4J4G
• 分子名称: Cyanovirin-N (2 entities in total)
• 機能のキーワード: cvnh fold, carbohydrate binding protein, antiviral protein, sugar binding protein
• 由来する生物種: Nostoc ellipsosporum
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 65892.16

構造登録者

Koharudin, L.M.I.,Liu, L.,Gronenborn, A.M. (登録日: 2013-02-06, 公開日: 2013-04-03, 最終更新日: 2023-09-20)

主引用文献

Koharudin, L.M.,Liu, L.,Gronenborn, A.M.
Different 3D domain-swapped oligomeric cyanovirin-N structures suggest trapped folding intermediates.
Proc.Natl.Acad.Sci.USA, 110:7702-7707, 2013

PubMed Abstract: Although it has long been established that the amino acid sequence encodes the fold of a protein, how individual proteins arrive at their final conformation is still difficult to predict, especially for oligomeric structures. Here, we present a comprehensive characterization of oligomeric species of cyanovirin-N that all are formed by a polypeptide chain with the identical amino acid sequence. Structures of the oligomers were determined by X-ray crystallography, and each one exhibits 3D domain swapping. One unique 3D domain-swapped structure is observed for the trimer, while for both dimer and tetramer, two different 3D domain-swapped structures were obtained. In addition to the previously identified hinge-loop region of the 3D domain-swapped dimer, which resides between strands β5 and β6 in the middle of the polypeptide sequence, another hinge-loop region is observed between strands β7 and β8 in the structures. Plasticity in these two regions allows for variability in dihedral angles and concomitant differences in chain conformation that results in the differently 3D domain-swapped multimers. Based on all of the different structures, we propose possible folding pathways for this protein. Altogether, our results illuminate the amazing ability of cyanovirin-N to proceed down different folding paths and provide general insights into oligomer formation via 3D domain swapping.

PubMed: 23610431
DOI: 10.1073/pnas.1300327110

実験手法

X-RAY DIFFRACTION (2.4 Å)