The crystal structure of ferritin from Chlorobium tepidum reveals a new conformation of the 4-fold channel for this protein family

Arenas-Salinas, Mauricio; Townsend, Philip D.; Brito, Christian; Márquez, Valeria; Marabolli, Vanessa; González‐Nilo, Fernando; Matias, Cata; Watt, Richard K.; López-Castro, Juan de Dios; Domínguez‐Vera, José M.; Pohl, Ehmke; Yévenes, Alejandro

doi:10.1016/j.biochi.2014.07.019

Cited by 13 publications

(14 citation statements)

References 47 publications

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“…They include Asp129 and Glu132 presenting in their narrowest area (Fig. 3C,F), consistent with previous reports [31]. Moreover, the threefold channels of Fer147 and PeFer are interlaced positive and negative regions of the electrostatic potential (Fig.…”

Section: Discussionsupporting

confidence: 91%

Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta

Ming

Huan

et al. 2021

FEBS Open Bio

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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.

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Section: Discussionsupporting

confidence: 91%

Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta

Ming

Huan

et al. 2021

FEBS Open Bio

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“…The 24 monomers in ferritin are organised to form a large octahedral capsule capable of storing and transporting iron oxide. The ferritin complex from Chlorobium tepidum is shown as an example in Supplementary Figure 1 48 .…”

Section: Resultsmentioning

confidence: 99%

Functional determinants of protein assembly into homomeric complexes

Bergendahl

Marsh

2017

Sci Rep

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Approximately half of proteins with experimentally determined structures can interact with other copies of themselves and assemble into homomeric complexes, the overwhelming majority of which (>96%) are symmetric. Although homomerisation is often assumed to a functionally beneficial result of evolutionary selection, there has been little systematic analysis of the relationship between homomer structure and function. Here, utilizing the large numbers of structures and functional annotations now available, we have investigated how proteins that assemble into different types of homomers are associated with different biological functions. We observe that homomers from different symmetry groups are significantly enriched in distinct functions, and can often provide simple physical and geometrical explanations for these associations in regards to substrate recognition or physical environment. One of the strongest associations is the tendency for metabolic enzymes to form dihedral complexes, which we suggest is closely related to allosteric regulation. We provide a physical explanation for why allostery is related to dihedral complexes: it allows for efficient propagation of conformational changes across isologous (i.e. symmetric) interfaces. Overall we demonstrate a clear relationship between protein function and homomer symmetry that has important implications for understanding protein evolution, as well as for predicting protein function and quaternary structure.

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“…Ferritin has a typical structure of a 24-subunit spherical protein encapsulating an iron oxide core (11). The subunit comprises two different types: FTH (21 kDa) and FTL (19 kDa) (12).…”

Section: Discussionmentioning

confidence: 99%

Ferritin: A potential serum marker for lymph node metastasis in head and neck squamous cell carcinoma

Wang

Han

et al. 2018

Oncol Lett

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Head and neck squamous cell carcinoma (HNSCC) is the sixth most common cancer in the world, yet current treatment options are associated with limited success. The aim of the present study was to investigate the expression of ferritin in HNSCC and clarify whether it may serve as a biomarker for predicting HNSCC metastasis. The chemiluminescent immunoassay method was used to investigate the differences in the serum ferritin (SF) levels between patients with and without tumors, and between HNSCC with and without lymph node metastasis. The iron content and expression levels of ferritin were detected to verify the differences between tumor and normal tissues, and between HNSCC without and with lymph node metastasis. Data from the Gene Expression Omnibus (GEO) dataset was used to support the aforementioned results. No statistically significant difference in the SF level was observed between patients with and without tumors. Iron content and expression levels of ferritin heavy chain (FTH) and ferritin light chain (FTL) were higher in tumor tissues compared with normal tissues. The iron content and expression levels of SF, FTH and FTL were increased in HNSCC with metastasis compared with HNSCC without metastasis. The GEO dataset further verified the results and reported that the expression level of FTH was correlated with the prognosis of patients with HNSCC. Ferritin may not be a biomarker for the early diagnosis of HNSCC. However, an association exists between the expression level of ferritin and HNSCC cervical metastasis. SF may be a potential biomarker for predicting cervical lymph node metastasis in patients with HNSCC.

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The crystal structure of ferritin from Chlorobium tepidum reveals a new conformation of the 4-fold channel for this protein family

Cited by 13 publications

References 47 publications

Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta

Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta

Functional determinants of protein assembly into homomeric complexes

Ferritin: A potential serum marker for lymph node metastasis in head and neck squamous cell carcinoma

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