2c3b
The Crystal Structure of Aspergillus fumigatus Cyclophilin reveals 3D Domain Swapping of a Central ElementThe Crystal Structure of Aspergillus fumigatus Cyclophilin reveals 3D Domain Swapping of a Central Element
Structural highlights
FunctionQ4WHY9_ASPFU PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU363019] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. The crystal structure of Aspergillus fumigatus cyclophilin reveals 3D domain swapping of a central element.,Limacher A, Kloer DP, Fluckiger S, Folkers G, Crameri R, Scapozza L Structure. 2006 Feb;14(2):185-95. PMID:16472738[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||