scholarly journals Structural Basis of the Metal Specificity for Nickel Regulatory Protein NikR†,‡

Biochemistry ◽  
2008 ◽  
Vol 47 (7) ◽  
pp. 1938-1946 ◽  
Author(s):  
Christine M. Phillips ◽  
Eric R. Schreiter ◽  
Yayi Guo ◽  
Sheila C. Wang ◽  
Deborah B. Zamble ◽  
...  
Keyword(s):  
Regulatory Protein ◽  
Structural Basis ◽  
Metal Specificity

Distinct Metal Environment in Fe-Substituted Manganese Superoxide Dismutase Provides a Structural Basis of Metal Specificity

1998 ◽  
Vol 120 (37) ◽  
pp. 9684-9685 ◽  
Author(s):  
Ross A. Edward ◽  
Mei M. Whittaker ◽  
James W. Whittaker ◽  
Geoffrey B. Jameson ◽  
Edward N. Baker
Keyword(s):  
Superoxide Dismutase ◽  
Manganese Superoxide Dismutase ◽  
Structural Basis ◽  
Metal Specificity ◽  
Manganese Superoxide

Efficient preparation and metal specificity of the regulatory protein TroR from the human pathogen Treponema pallidum

Metallomics ◽  
2013 ◽  
Vol 5 (10) ◽  
pp. 1448 ◽  
Author(s):  
Yi Liu ◽  
Wei Li ◽  
Yaozhu Wei ◽  
Yindi Jiang ◽  
Xiangshi Tan
Keyword(s):  
Regulatory Protein ◽  
Treponema Pallidum ◽  
Human Pathogen ◽  
Metal Specificity

scholarly journals Asymmetrically Positioned Flagellar Control Units Regulate Human Sperm Rotation

2018 ◽  
Author(s):  
Melissa R. Miller ◽  
Samuel J Kenny ◽  
Nadja Mannowetz ◽  
Steven A. Mansell ◽  
Michal Wojcik ◽  
...  
Keyword(s):  
Ion Channels ◽  
Regulatory Protein ◽  
Super Resolution ◽  
Human Sperm ◽  
Regulatory Proteins ◽  
Proton Channel ◽  
Structural Basis ◽  
Control Units ◽  
Proton Transporters ◽  
Super Resolution Microscopy

AbstractThe ability of sperm to fertilize an egg is controlled by ion channels, one of which is the pH-dependent calcium channel of sperm CatSper. For CatSper to be fully activated, the cytoplasmic pH must be alkaline, which is accomplished by either proton transporters, or a faster mechanism, such as the voltage-gated proton channel Hv1. To ensure effective regulation, these channels and regulatory proteins must be tightly compartmentalized. Here, we characterize human sperm nanodomains that are comprised of Hv1, CatSper and regulatory protein ABHD2. Super-resolution microscopy revealed that Hv1 forms asymmetrically positioned bilaterally distributed longitudinal lines that span the entire length of the sperm tail. Such a distribution provides a direct structural basis for the selective activation of CatSper, and subsequent flagellar rotation along the long axis that, together with hyperactivated motility, enhances sperm fertility. Indeed, Hv1 inhibition leads to a decrease in sperm rotation. Thus, sperm ion channels are organized in distinct regulatory nanodomains that control hyperactivated motility and rotation.

scholarly journals Cysteine Oxidation Regulates the RNA-Binding Activity of Iron Regulatory Protein 2

2009 ◽  
Vol 29 (8) ◽  
pp. 2219-2229 ◽  
Author(s):  
Kimberly B. Zumbrennen ◽  
Michelle L. Wallander ◽  
S. Joshua Romney ◽  
Elizabeth A. Leibold
Keyword(s):  
Oxidative Stress ◽  
Transferrin Receptor ◽  
Iron Homeostasis ◽  
Rna Binding ◽  
Regulatory Protein ◽  
Binding Activity ◽  
Structural Basis ◽  
Iron Regulatory Protein ◽  
Transferrin Receptor 1 ◽  
Binding Cleft

ABSTRACT Iron regulatory protein 2 (IRP2) is an RNA-binding protein that regulates the posttranscriptional expression of proteins required for iron homeostasis such as ferritin and transferrin receptor 1. IRP2 RNA-binding activity is primarily regulated by iron-mediated proteasomal degradation, but studies have suggested that IRP2 RNA binding is also regulated by thiol oxidation. We generated a model of IRP2 bound to RNA and found that two cysteines (C512 and C516) are predicted to lie in the RNA-binding cleft. Site-directed mutagenesis and thiol modification show that, while IRP2 C512 and C516 do not directly interact with RNA, both cysteines are located within the RNA-binding cleft and must be unmodified/reduced for IRP2-RNA interactions. Oxidative stress induced by cellular glucose deprivation reduces the RNA-binding activity of IRP2 but not IRP2-C512S or IRP2-C516S, consistent with the formation of a disulfide bond between IRP2 C512 and C516 during oxidative stress. Decreased IRP2 RNA binding is correlated with reduced transferrin receptor 1 mRNA abundance. These studies provide insight into the structural basis for IRP2-RNA interactions and reveal an iron-independent mechanism for regulating iron homeostasis through the redox regulation of IRP2 cysteines.

scholarly journals Structural Basis of Reversible Phosphorylation by Maize Pyruvate Orthophosphate Dikinase Regulatory Protein

2015 ◽  
Vol 170 (2) ◽  
pp. 732-741 ◽  
Author(s):  
Lun Jiang ◽  
Yi-bo Chen ◽  
Jiangge Zheng ◽  
Zhenhang Chen ◽  
Yujie Liu ◽  
...  
Keyword(s):  
Regulatory Protein ◽  
Structural Basis ◽  
Reversible Phosphorylation ◽  
Pyruvate Orthophosphate Dikinase ◽  
Orthophosphate Dikinase

scholarly journals Structural Basis for the Regulation of N-Acetylglutamate Kinase by PII in Arabidopsis thaliana

2007 ◽  
Vol 282 (49) ◽  
pp. 35733-35740 ◽  
Author(s):  
Yutaka Mizuno ◽  
Greg B. G. Moorhead ◽  
Kenneth K.-S. Ng
Keyword(s):  
Arabidopsis Thaliana ◽  
Feedback Inhibition ◽  
Regulatory Protein ◽  
Enzyme Regulation ◽  
Inhibitory Effect ◽  
Structural Basis ◽  
Atp Binding Site ◽  
Domains Of Life ◽  
Substrate Binding Sites ◽  
Acetylglutamate Kinase

PII is a highly conserved regulatory protein found in organisms across the three domains of life. In cyanobacteria and plants, PII relieves the feedback inhibition of the rate-limiting step in arginine biosynthesis catalyzed by N-acetylglutamate kinase (NAGK). To understand the molecular structural basis of enzyme regulation by PII, we have determined a 2.5-Å resolution crystal structure of a complex formed between two homotrimers of PII and a single hexamer of NAGK from Arabidopsis thaliana bound to the metabolites N-acetylglutamate, ADP, ATP, and arginine. In PII, the T-loop and Trp22 at the start of the α1-helix, which are both adjacent to the ATP-binding site of PII, contact two β-strands as well as the ends of two central helices (αE and αG) in NAGK, the opposing ends of which form major portions of the ATP and N-acetylglutamate substrate-binding sites. The binding of Mg2+·ATP to PII stabilizes a conformation of the T-loop that favors interactions with both open and closed conformations of NAGK. Interactions between PII and NAGK appear to limit the degree of opening and closing of the active-site cleft in opposition to a domain-separating inhibitory effect exerted by arginine, thus explaining the stimulatory effect of PII on the kinetics of arginine-inhibited NAGK.

scholarly journals Structural Basis for Activation of the Cytoskeleton Regulatory Protein IRSp53

2012 ◽  
Vol 102 (3) ◽  
pp. 697a
Author(s):  
David J.E. Kast ◽  
Yadaiah Madasu ◽  
Malgorzata Boczkowska ◽  
Grzegorz Rebowski ◽  
Roberto Dominguez
Keyword(s):  
Regulatory Protein ◽  
Structural Basis
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