6LPD

Phascolosoma esculenta

Summary for 6LPD

• Entry DOI: 10.2210/pdb6lpd/pdb
• Descriptor: Ferritin, FE (II) ION, FE (III) ION, ... (4 entities in total)
• Functional Keywords: phascolosoma esculenta (fer147), ferritin, structural protein, oxidoreductase
• Biological source: Phascolosoma esculenta
• Total number of polymer chains: 6
• Total formula weight: 123342.53

Authors

Su, X.R.,Ming, T.H. (deposition date: 2020-01-09, release date: 2021-01-13, Last modification date: 2023-11-29)

Primary citation

Ming, T.,Huan, H.,Su, C.,Huo, C.,Wu, Y.,Jiang, Q.,Qiu, X.,Lu, C.,Zhou, J.,Li, Y.,Su, X.
Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta.
Febs Open Bio, 11:793-803, 2021

PubMed Abstract: For marine invertebrates with no adaptive immune system, ferritin is a major intracellular iron-storage protein with a critical role in innate immunity. Here, we present the crystal structures of two novel ferritins [Fer147 and Phascolosoma esculenta ferritin (PeFer)] from the marine invertebrate P. esculenta, which resides in muddy-bottom coastal regions. Fer147 and PeFer exhibit the 4-3-2 symmetry of cage-like hollow shells containing 24 subunits, similar to other known ferritins. Fer147 and PeFer contain both the conserved ferroxidase center and threefold channels. Subtle structural differences in the putative nucleation sites suggest possible routes of metal ion movement in the protein shells. However, the marked variation in the electrostatic potential of the threefold channels in Fer147 and the fourfold channels in PeFer suggests significant diversity between Fer147 and PeFer in terms of metal ion aggregation and cation exclusion. In summary, the presented crystal structures may serve as references for studies of the iron-storage mechanism of additional ferritins from marine invertebrates.

PubMed: 33448656
DOI: 10.1002/2211-5463.13080

Experimental method

X-RAY DIFFRACTION (1.65 Å)