scholarly journals Crystal structure of the DENR-MCT-1 complex revealed zinc-binding site essential for heterodimer formation

2018 ◽  
Vol 116 (2) ◽  
pp. 528-533 ◽  
Author(s):  
Ivan B. Lomakin ◽  
Sergey E. Dmitriev ◽  
Thomas A. Steitz
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Translation Initiation ◽  
Zinc Ion ◽  
Zinc Binding ◽  
Ion Binding ◽  
Binding Interface ◽  
Zinc Binding Site ◽  
Reading Frames ◽  
Zinc Ion Binding

The density-regulated protein (DENR) and the malignant T cell-amplified sequence 1 (MCT-1/MCTS1) oncoprotein support noncanonical translation initiation, promote translation reinitiation on a specific set of mRNAs with short upstream reading frames, and regulate ribosome recycling. DENR and MCT-1 form a heterodimer, which binds to the ribosome. We determined the crystal structure of the heterodimer formed by human MCT-1 and the N-terminal domain of DENR at 2.0-Å resolution. The structure of the heterodimer reveals atomic details of the mechanism of DENR and MCT-1 interaction. Four conserved cysteine residues of DENR (C34, C37, C44, C53) form a classical tetrahedral zinc ion-binding site, which preserves the structure of the DENR’s MCT-1–binding interface that is essential for the dimerization. Substitution of all four cysteines by alanine abolished a heterodimer formation. Our findings elucidate further the mechanism of regulation of DENR-MCT-1 activities in unconventional translation initiation, reinitiation, and recycling.

scholarly journals The crystal structure of mammalian inositol 1,3,4,5,6-pentakisphosphate 2-kinase reveals a new zinc-binding site and key features for protein function

2017 ◽  
Vol 292 (25) ◽  
pp. 10534-10548 ◽  
Author(s):  
Elsa Franco-Echevarría ◽  
Julia Sanz-Aparicio ◽  
Charles A. Brearley ◽  
Juana M. González-Rubio ◽  
Beatriz González
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Protein Function ◽  
Zinc Binding ◽  
Zinc Binding Site ◽  
Key Features

Crystal Structure of Streptococcus dysgalactiae-Derived Mitogen Reveals a Zinc-Binding Site and Alterations in TcR Binding

2007 ◽  
Vol 373 (5) ◽  
pp. 1089-1097 ◽  
Author(s):  
Susanna Saarinen ◽  
Hidehito Kato ◽  
Takehiko Uchiyama ◽  
Tohru Miyoshi-Akiyama ◽  
Anastassios C. Papageorgiou
Keyword(s):  
Crystal Structure ◽  
Binding Site ◽  
Zinc Binding ◽  
Streptococcus Dysgalactiae ◽  
Zinc Binding Site

scholarly journals The Crystal Structure of Hepatitis C Virus NS3 Proteinase Reveals a Trypsin-like Fold and a Structural Zinc Binding Site

Cell ◽  
1996 ◽  
Vol 87 (2) ◽  
pp. 331-342 ◽  
Author(s):  
Robert A Love ◽  
Hans E Parge ◽  
John A Wickersham ◽  
Zdenek Hostomsky ◽  
Noriyuki Habuka ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Binding Site ◽  
Zinc Binding ◽  
Zinc Binding Site

scholarly journals Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site

Structure ◽  
1995 ◽  
Vol 3 (8) ◽  
pp. 769-779 ◽  
Author(s):  
Anastassios C Papageorgiou ◽  
K.Ravi Acharya ◽  
Robert Shapiro ◽  
Edward F Passalacqua ◽  
Rossalyn D Brehm ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Staphylococcus Aureus ◽  
Binding Site ◽  
Zinc Binding ◽  
Zinc Binding Site

Crystal Structure of a Zinc-Activated Variant of Human Carbonic Anhydrase I, CA I Michigan 1:  Evidence for a Second Zinc Binding Site Involving Arginine Coordination

Biochemistry ◽  
2002 ◽  
Vol 41 (20) ◽  
pp. 6237-6244 ◽  
Author(s):  
Marta Ferraroni ◽  
Silvia Tilli ◽  
Fabrizio Briganti ◽  
W. Richard Chegwidden ◽  
Claudiu T. Supuran ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Carbonic Anhydrase ◽  
Binding Site ◽  
Zinc Binding ◽  
Carbonic Anhydrase I ◽  
Zinc Binding Site ◽  
Human Carbonic Anhydrase

Unravelling the inhibitory zinc ion binding site and the metal exchange mechanism in human DPP III

2021 ◽  
Author(s):  
Antonija Tomić ◽  
Hrvoje Brkić ◽  
Antonia Matić ◽  
Sanja Tomić
Keyword(s):  
Binding Site ◽  
Dipeptidyl Peptidase ◽  
Zinc Ion ◽  
Exchange Mechanism ◽  
Ion Binding ◽  
Metal Exchange ◽  
Human Tissues ◽  
Protein Catabolism ◽  
Almost All ◽  
Zinc Ion Binding

Dipeptidyl peptidase III (DPP III), a zinc-dependent exopeptidase, is widely distributed in organisms and present in almost all human tissues. In addition to its involvement in protein catabolism, it plays...

scholarly journals Structural studies of neuropilin-2 reveal a zinc ion binding site remote from the vascular endothelial growth factor binding pocket

FEBS Journal ◽  
2016 ◽  
Vol 283 (10) ◽  
pp. 1921-1934 ◽  
Author(s):  
Yi-Chun Isabella Tsai ◽  
Constantina Fotinou ◽  
Rohini Rana ◽  
Tamas Yelland ◽  
Paul Frankel ◽  
...  
Keyword(s):  
Vascular Endothelial Growth Factor ◽  
Growth Factor ◽  
Binding Site ◽  
Binding Pocket ◽  
Zinc Ion ◽  
Ion Binding ◽  
Vascular Endothelial ◽  
Structural Studies ◽  
Endothelial Growth Factor ◽  
Zinc Ion Binding

scholarly journals SARS-CoV-2 Mpro inhibition by zinc ion: structural features and hints for drug design

2021 ◽  
Author(s):  
Deborah Grifagni ◽  
Vito Calderone ◽  
Stefano Giuntini ◽  
Francesca Cantini ◽  
Marco Fragai ◽  
...  
Keyword(s):  
Drug Design ◽  
Binding Site ◽  
Structural Data ◽  
Structural Features ◽  
Zinc Ion ◽  
Zinc Binding ◽  
Main Protease ◽  
Zinc Binding Site ◽  
Organic Inhibitor

Structural data on SARS-CoV-2 main protease in complex with a zinc-containing organic inhibitor gave hints on the presence of a zinc binding site involving the catalytic relevant cysteine and histidine...

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