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4J4D

Structure of P51G Cyanovirin-N swapped dimer in the P21212 space group

Summary for 4J4D
Entry DOI10.2210/pdb4j4d/pdb
Related4J4C 4J4E 4J4F 4J4G
DescriptorCyanovirin-N (2 entities in total)
Functional Keywordscvnh fold, carbohydrate binding protein, antiviral protein, sugar binding protein
Biological sourceNostoc ellipsosporum
Total number of polymer chains4
Total formula weight43928.10
Authors
Koharudin, L.M.I.,Liu, L.,Gronenborn, A.M. (deposition date: 2013-02-06, release date: 2013-04-03, Last modification date: 2024-11-06)
Primary citationKoharudin, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

227561

數據於2024-11-20公開中

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