scholarly journals Structure of the lutein-binding domain of human StARD3 at 1.74 Å resolution and model of a complex with lutein

2016 ◽  
Vol 72 (8) ◽  
pp. 609-618 ◽  
Author(s):  
Martin P. Horvath ◽  
Evan W. George ◽  
Quang T. Tran ◽  
Kody Baumgardner ◽  
Gabe Zharov ◽  
...  
Keyword(s):  
Lipid Transfer Protein ◽  
Transport Proteins ◽  
Binding Domain ◽  
Regions Of Interest ◽  
The Other ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Biochemical Function ◽  
Rigid Body Docking ◽  
Resolution Structure

A crystal structure of the lutein-binding domain of human StARD3 (StAR-related lipid-transfer protein 3; also known as MLN64) has been refined to 1.74 Å resolution. A previous structure of the same protein determined to 2.2 Å resolution highlighted homology with StARD1 and shared cholesterol-binding character. StARD3 has since been recognized as a carotenoid-binding protein in the primate retina, where its biochemical function of binding lutein with specificity appears to be well suited to recruit this photoprotective molecule. The current and previous structures correspond closely to each other (r.m.s.d. of 0.25 Å), especially in terms of the helix-grip fold constructed around a solvent-filled cavity. Regions of interest were defined with alternate conformations in the current higher-resolution structure, including Arg351 found within the cavity and Ω1, a loop of four residues found just outside the cavity entrance. Models of the complex with lutein generated by rigid-body docking indicate that one of the ionone rings must protrude outside the cavity, and this insight has implications for molecular interactions with transport proteins and enzymes that act on lutein. Interestingly, models with the ∊-ionone ring characteristic of lutein pointing towards the bottom of the cavity were associated with fewer steric clashes, suggesting that steric complementarity and ligand asymmetry may play a role in discriminating lutein from the other ocular carotenoids zeaxanthin andmeso-zeaxanthin, which only have β-ionone rings.

scholarly journals Miro recruits VPS13D to mitochondria

2020 ◽  
Author(s):  
Andrés Guillén-Samander ◽  
Marianna Leonzino ◽  
Pietro De Camilli
Keyword(s):  
Secretory Pathway ◽  
Lipid Transfer Protein ◽  
Transport Proteins ◽  
Lipid Transport ◽  
Eukaryotic Cells ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Accessory Factor ◽  
Mitochondrial Motility ◽  
Higher Eukaryotes

AbstractMitochondria, which are excluded from the secretory pathway, depend on lipid transport proteins for their lipid supply from the ER, where most lipids are synthesized. In yeast, the outer membrane GTPase Gem1 is an accessory factor of ERMES, an ER-mitochondria tethering complex that contains lipid transport domains and plays a function, partially redundant with VPS13, in lipid transfer between the two organelles. In metazoa, where VPS13, but not ERMES, is present, the Gem1 orthologue Miro has been linked to mitochondrial motility but not to lipid transport. Here we show that Miro recruits to mitochondria the lipid transport protein VPS13D which, like Miro, is an essential protein in mammals, and whose localization had remained elusive. We also show that VPS13D can tether mitochondria to the ER in a Miro- and VAP-dependent way. These findings reveal a so far missing link between function(s) of Gem1/Miro in yeast and higher eukaryotes, where Miro is a Parkin substrate, with potential implications for Parkinson’s disease pathogenesis.SummaryProtein-mediated ER-mitochondria lipid transfer is critical for eukaryotic cells. However, the underlying machinery is not well conserved. Guillén-Samander et al, show that Gem1/Miro is an evolutionary conserved link between the yeast ERMES complex and the mammalian lipid transfer protein VPS13D.

scholarly journals The key to the allergenicity of lipid transfer protein (LTP) ligands: A structural characterization

2021 ◽  
pp. 158928
Author(s):  
Zulema Gonzalez-Klein ◽  
Bruno Cuevas-Zuviria ◽  
Andrea Wangorsch ◽  
Guadalupe Hernandez-Ramirez ◽  
Diego Pazos-Castro ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein

scholarly journals Structural Characterization of Act c 10.0101 and Pun g 1.0101—Allergens from the Non-Specific Lipid Transfer Protein Family

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 256
Author(s):  
Andrea O’Malley ◽  
Swanandi Pote ◽  
Ivana Giangrieco ◽  
Lisa Tuppo ◽  
Anna Gawlicka-Chruszcz ◽  
...  
Keyword(s):  
Immunoglobulin E ◽  
Lipid Transfer Protein ◽  
Mass Spectrometry Analysis ◽  
Lipid Transfer ◽  
Helical Structures ◽  
Spectrometry Analysis ◽  
X Ray Crystallography ◽  
Transfer Protein ◽  
Specific Lipid

(1) Background: Non-specific lipid transfer proteins (nsLTPs), which belong to the prolamin superfamily, are potent allergens. While the biological role of LTPs is still not well understood, it is known that these proteins bind lipids. Allergen nsLTPs are characterized by significant stability and resistance to digestion. (2) Methods: nsLTPs from gold kiwifruit (Act c 10.0101) and pomegranate (Pun g 1.0101) were isolated from their natural sources and structurally characterized using X-ray crystallography (3) Results: Both proteins crystallized and their crystal structures were determined. The proteins have a very similar overall fold with characteristic compact, mainly α-helical structures. The C-terminal sequence of Act c 10.0101 was updated based on our structural and mass spectrometry analysis. Information on proteins’ sequences and structures was used to estimate the risk of cross-reactive reactions between Act c 10.0101 or Pun g 1.0101 and other allergens from this family of proteins. (4) Conclusions: Structural studies indicate a conformational flexibility of allergens from the nsLTP family and suggest that immunoglobulin E binding to some surface regions of these allergens may depend on ligand binding. Both Act c 10.0101 and Pun g 1.0101 are likely to be involved in cross-reactive reactions involving other proteins from the nsLTP family.

Structural Stability and Surface Activity of Sunflower 2S Albumins and Nonspecific Lipid Transfer Protein

2010 ◽  
Vol 58 (10) ◽  
pp. 6490-6497 ◽  
Author(s):  
Bernadett Berecz ◽  
E. N. Clare Mills ◽  
László Tamás ◽  
Ferenc Láng ◽  
Peter R. Shewry ◽  
...  
Keyword(s):  
Structural Stability ◽  
Surface Activity ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
2S Albumins ◽  
Nonspecific Lipid Transfer Protein
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