2C3B

The Crystal Structure of Aspergillus fumigatus Cyclophilin reveals 3D Domain Swapping of a Central Element

Summary for 2C3B

• Entry DOI: 10.2210/pdb2c3b/pdb
• Descriptor: PPIASE, SULFATE ION (3 entities in total)
• Functional Keywords: isomerase, 3d domain swapping, misfolding, ppiase, asp f 11, allergen, rotamase
• Biological source: ASPERGILLUS FUMIGATUS
• Total number of polymer chains: 2
• Total formula weight: 37988.52

Authors

Limacher, A.,Kloer, D.P.,Fluckiger, S.,Folkers, G.,Crameri, R.,Scapozza, L. (deposition date: 2005-10-05, release date: 2006-01-30, Last modification date: 2024-11-13)

Primary citation

Limacher, A.,Kloer, D.P.,Fluckiger, S.,Folkers, G.,Crameri, R.,Scapozza, L.
The Crystal Structure of Aspergillus Fumigatus Cyclophilin Reveals 3D Domain Swapping of a Central Element
Structure, 14:185-, 2006

PubMed Abstract: The crystal structure of Aspergillus fumigatus cyclophilin (Asp f 11) was solved by the multiwavelength anomalous dispersion method and was refined to a resolution of 1.85 A with R and R(free) values of 18.9% and 21.4%, respectively. Many cyclophilin structures have been solved to date, all showing the same monomeric conformation. In contrast, the structure of A. fumigatus cyclophilin reveals dimerization by 3D domain swapping and represents one of the first proteins with a swapped central domain. The domain-swapped element consists of two beta strands and a subsequent loop carrying a conserved tryptophan. The tryptophan binds into the active site, inactivating cis-trans isomerization. This might be a means of biological regulation. The two hinge loops leave the protein prone to misfolding. In this context, alternative forms of 3D domain swapping that can lead to N- or C-terminally swapped dimers, oligomers, and aggregates are discussed.

PubMed: 16472738
DOI: 10.1016/J.STR.2005.10.015

Experimental method

X-RAY DIFFRACTION (1.85 Å)