Iron Transport in Living Cells

Crumbliss, Alvin L.; Siburt, Claire J. Parker

doi:10.1002/9781118165850.ch13

Cited by 2 publications

(3 citation statements)

References 185 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The synergistic anion has been shown to preorganize the binding site prior to iron insertion for FbpA, 51 and to control the release of iron, because proton-assisted release of the phosphate anion is the preliminary step in iron release. 52 In addition, synergistic anion exchange may be an important regulator in iron delivery by FbpA to the cytosol 22 while the kinetics of synergistic anion exchange is affected by concentration and identity of background electrolyte. 31,52,53 However, it can be seen that three Tyrs and a carbonate coordinate to iron in FbpA from Mannheimia haemolyticafour, 54 while only four Tyrs and one His were the iron-binding ligands without synergistic anion in FbpA from Campylobacter jejuni.…”

Section: Discussionmentioning

confidence: 99%

“…52 In addition, synergistic anion exchange may be an important regulator in iron delivery by FbpA to the cytosol 22 while the kinetics of synergistic anion exchange is affected by concentration and identity of background electrolyte. 31,52,53 However, it can be seen that three Tyrs and a carbonate coordinate to iron in FbpA from Mannheimia haemolyticafour, 54 while only four Tyrs and one His were the iron-binding ligands without synergistic anion in FbpA from Campylobacter jejuni. 55 Besides Fe 3+ , Ga 3+ and Bi 3+ , but not Co 3+ , can display to a certain extent affinity toward apo-FbpA.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Binding of oxo-Cu2 clusters to ferric ion-binding protein A from Neisseria gonorrhoeae: a structural insight

Chen

Wang

et al. 2013

Metallomics

View full text Add to dashboard Cite

The ferric ion-binding protein A (FbpA), a member of transferrin superfamily, is a periplasmic iron transporter employed by many Gram-negative pathogens. Our experiments indicated copper(ii) could bind with Neisseria gonorrhoeae FbpA (NgFbpA), and the binding constant reached up to (8.7 ± 0.2) × 10(8) M(-1)via UV-vis titration. The crystal structure of recombinant Cu-NgFbpA at 2.1 Å revealed that the oxo-Cu2 clusters (dinuclear centres) assembled in the iron binding cleft and were bound to the two adjacent tyrosine residues (Y195 and Y196) of the protein, two Cu ions coordinated with two tyrosines, Y195 and Y196, respectively, which was different from the binding model of Fe ion with FbpA, in which Y195 and Y196 coordinated together with one Fe ion. While this was similar to the binding of Zr and Hf ion clusters, Y195 and Y196 coordinated with two metal ions and the μ-oxo-bridges linking the metal ions. Structural superimposition demonstrated that oxo-Cu2-NgFbpA still keeping an open conformation, similar to the apo-form of NgFbpA. The structure presented additional information towards an understanding of the function of FbpA, and provided a detailed binding model for FbpA protein with the possible metal ions in a biological system.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Binding of oxo-Cu2 clusters to ferric ion-binding protein A from Neisseria gonorrhoeae: a structural insight

Chen

Wang

et al. 2013

Metallomics

View full text Add to dashboard Cite

show abstract

“…A similar conclusion is obtained from the sequence studies for tropomiosin (Stone and Smillie, 1978 ) and troponin (Pearstone et al, 1976 ) (that bind to actin), and titin (Maruyama et al, 1981 ) (that binds to myosin). These studies reveal that the sarcomeric polymers are all weak polyanions, and therefore programmed to be mutually repulsive unless the fixed anionic charges are connected by the hypothetical “salt bridge,” as claimed by the sliding filament model, or screened by interaction with mobile ions (Manning, 1978 ; Yang and Janmey, 1996 ; Xian et al, 1999 ; Ciferri and Perico, 2010 ; Ciferri, 2012a ; Crumbliss and Parker Siburt, 2012 ; Maglio et al, 2012 ). The latter possibility has not been previously considered, but should not be neglected.…”

Section: Analysis Of Self-assembling Contributionsmentioning

confidence: 99%

The Assembling and Contraction Mechanisms of Striated Muscles

Ciferri

Crumbliss

2018

Front. Chem.

Self Cite

View full text Add to dashboard Cite

A novel approach to the description of the assembly mechanism of functional biological structures is presented. The approach is based on the identification of fundamental self-assembling processes to which an additional structurization “engineered” by Nature to optimize functions is superimposed. Application of the approach to the structure and contraction of the striated muscle evidences a key role of the residual liquid crystallinity of a constrained structure and the alteration of the compatibility between the thin and thick filaments driven by ionic interactions. ATP hydrolysis boosts the relaxation process. A strong protein scaffold, engineered during the evolutionary process and based on the selective anchoring of coordinated filaments, directs a demixing tendency of the two filaments toward a sliding motion along the fiber axis. The Huxley-Hanson sliding filament hypothesis aimed to explain the contraction-relaxation function of the striated muscle, but does not offer any clue on the overall assembling mechanism of the myofibril.

show abstract

Iron Transport in Living Cells

Cited by 2 publications

References 185 publications

Binding of oxo-Cu2 clusters to ferric ion-binding protein A from Neisseria gonorrhoeae: a structural insight

Binding of oxo-Cu2 clusters to ferric ion-binding protein A from Neisseria gonorrhoeae: a structural insight

The Assembling and Contraction Mechanisms of Striated Muscles

Contact Info

Product

Resources

About