Erratum to “Enhanced FTase activity achieved via piperazine interaction with catalytic zinc” [Bioorg. Med. Chem. Lett. 16 (2006) 984–988]

2006 ◽  
Vol 16 (8) ◽  
pp. 2312
Author(s):  
F. George Njoroge ◽  
Bancha Vibulbhan ◽  
Patrick Pinto ◽  
Corey Strickland ◽  
W. Robert Bishop ◽  
...  
Keyword(s):  
Catalytic Zinc ◽  
Ftase Activity

Enhanced FTase activity achieved via piperazine interaction with catalytic zinc

2006 ◽  
Vol 16 (4) ◽  
pp. 984-988 ◽  
Author(s):  
F. George Njoroge ◽  
Bancha Vibulbhan ◽  
Patrick Pinto ◽  
Corey Strickland ◽  
W. Robert Bishop ◽  
...  
Keyword(s):  
Catalytic Zinc ◽  
Ftase Activity

Enhanced FTase Activity Achieved via Piperazine Interaction with Catalytic Zinc.

ChemInform ◽  
2006 ◽  
Vol 37 (20) ◽  
Author(s):  
F. George Njoroge ◽  
Bancha Vibulbhan ◽  
Patrick Pinto ◽  
Corey Strickland ◽  
W. Robert Bishop ◽  
...  
Keyword(s):  
Catalytic Zinc ◽  
Ftase Activity

scholarly journals The crystal structure of a 250-kDa heterotetrameric particle explains inhibition of sheddase meprin β by endogenous fetuin-B

2021 ◽  
Vol 118 (14) ◽  
pp. e2023839118
Author(s):  
Ulrich Eckhard ◽  
Hagen Körschgen ◽  
Nele von Wiegen ◽  
Walter Stöcker ◽  
F. Xavier Gomis-Rüth
Keyword(s):  
Crystal Structure ◽  
Glycan Structure ◽  
Type I ◽  
Zinc Ions ◽  
Transmembrane Segment ◽  
Protein Inhibitor ◽  
Catalytic Domains ◽  
Endogenous Protein ◽  
Switch Mechanism ◽  
Catalytic Zinc

Meprin β (Mβ) is a multidomain type-I membrane metallopeptidase that sheds membrane-anchored substrates, releasing their soluble forms. Fetuin-B (FB) is its only known endogenous protein inhibitor. Herein, we analyzed the interaction between the ectodomain of Mβ (MβΔC) and FB, which stabilizes the enzyme and inhibits it with subnanomolar affinity. The MβΔC:FB crystal structure reveals a ∼250-kDa, ∼160-Å polyglycosylated heterotetrameric particle with a remarkable glycan structure. Two FB moieties insert like wedges through a “CPDCP trunk” and two hairpins into the respective peptidase catalytic domains, blocking the catalytic zinc ions through an “aspartate switch” mechanism. Uniquely, the active site clefts are obstructed from subsites S4 to S10′, but S1 and S1′ are spared, which prevents cleavage. Modeling of full-length Mβ reveals an EGF-like domain between MβΔC and the transmembrane segment that likely serves as a hinge to transit between membrane-distal and membrane-proximal conformations for inhibition and catalysis, respectively.

scholarly journals In silico design of potentially functional artificial metallo-haloalkane dehalogenase containing catalytic zinc

3 Biotech ◽  
2018 ◽  
Vol 8 (7) ◽  
Author(s):  
Thiau-Fu Ang ◽  
Abu Bakar Salleh ◽  
Yahaya M. Normi ◽  
Thean Chor Leow
Keyword(s):  
In Silico ◽  
Haloalkane Dehalogenase ◽  
In Silico Design ◽  
Catalytic Zinc

scholarly journals Probing the Role of Divalent Metal Ions in a Bacterial Psychrophilic Metalloprotease: Binding Studies of an Enzyme in the Crystalline State by X-Ray Crystallography

2003 ◽  
Vol 185 (14) ◽  
pp. 4195-4203 ◽  
Author(s):  
Stephanie Ravaud ◽  
Patrice Gouet ◽  
Richard Haser ◽  
Nushin Aghajari
Keyword(s):  
Metal Ions ◽  
Calcium Ions ◽  
Calcium Ion ◽  
Crystalline State ◽  
Zinc Ion ◽  
Binding Studies ◽  
X Ray ◽  
X Ray Crystallography ◽  
Catalytic Zinc

ABSTRACT The psychrophilic alkaline metalloprotease (PAP) produced by a Pseudomonas bacterium isolated in Antarctica belongs to the clan of metzincins, for which a zinc ion is essential for catalytic activity. Binding studies in the crystalline state have been performed by X-ray crystallography in order to improve the understanding of the role of the zinc and calcium ions bound to this protease. Cocrystallization and soaking experiments with EDTA in a concentration range from 1 to 85 mM have resulted in five three-dimensional structures with a distinct number of metal ions occupying the ion-binding sites. Evolution of the structural changes observed in the vicinity of each cation-binding site has been studied as a function of the concentration of EDTA, as well as of time, in the presence of the chelator. Among others, we have found that the catalytic zinc ion was the first ion to be chelated, ahead of a weakly bound calcium ion (Ca 700) exclusive to the psychrophilic enzyme. Upon removal of the catalytic zinc ion, the side chains of the active-site residues His-173, His-179 and Tyr-209 shifted ∼4, 1.0, and 1.6 Å, respectively. Our studies confirm and also explain the sensitivity of PAP toward moderate EDTA concentrations and propose distinct roles for the calcium ions. A new crystal form of native PAP validates our previous predictions regarding the adaptation of this enzyme to cold environments as well as the proteolytic domain calcium ion being exclusive for PAP independent of crystallization conditions.

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