The Phe-Ile Zipper: A Specific Interaction Motif Drives Antiparallel Coiled-Coil Hexamer Formation

Biochemistry ◽  
2017 ◽  
Vol 56 (40) ◽  
pp. 5300-5308 ◽  
Author(s):  
Ryan K. Spencer ◽  
Allon I. Hochbaum
Keyword(s):  
Specific Interaction ◽  
Coiled Coil ◽  
Antiparallel Coiled Coil

scholarly journals Antiparallel Coiled-Coil Interactions Mediate the Homodimerization of the DNA Damage-Repair Protein PALB2

Biochemistry ◽  
2018 ◽  
Vol 57 (47) ◽  
pp. 6581-6591 ◽  
Author(s):  
Fei Song ◽  
Minxing Li ◽  
Gaohua Liu ◽  
G.V.T. Swapna ◽  
Nourhan S. Daigham ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Damage Repair ◽  
Coiled Coil ◽  
Damage Repair ◽  
Repair Protein ◽  
Antiparallel Coiled Coil

scholarly journals Cadaverine Covalently Linked to Peptidoglycan Is Required for Interaction between the Peptidoglycan and the Periplasm-Exposed S-Layer-Homologous Domain of Major Outer Membrane Protein Mep45 in Selenomonas ruminantium

2010 ◽  
Vol 192 (22) ◽  
pp. 5953-5961 ◽  
Author(s):  
Seiji Kojima ◽  
Kyong-Cheol Ko ◽  
Yumiko Takatsuka ◽  
Naoki Abe ◽  
Jun Kaneko ◽  
...  
Keyword(s):  
Cell Surface ◽  
Surface Structure ◽  
Outer Membrane ◽  
Specific Interaction ◽  
Coiled Coil ◽  
Major Protein ◽  
Rich Region ◽  
Selenomonas Ruminantium ◽  
Covalently Linked ◽  
Cell Surface Structure

ABSTRACT The peptidoglycan of Selenomonas ruminantium is covalently bound to cadaverine (PG-cadaverine), which likely plays a significant role in maintaining the integrity of the cell surface structure. The outer membrane of this bacterium contains a 45-kDa major protein (Mep45) that is a putative peptidoglycan-associated protein. In this report, we determined the nucleotide sequence of the mep45 gene and investigated the relationship between PG-cadaverine, Mep45, and the cell surface structure. Amino acid sequence analysis showed that Mep45 is comprised of an N-terminal S-layer-homologous (SLH) domain followed by α-helical coiled-coil region and a C-terminal β-strand-rich region. The N-terminal SLH domain was found to be protruding into the periplasmic space and was responsible for binding to peptidoglycan. It was determined that Mep45 binds to the peptidoglycan in a manner dependent on the presence of PG-cadaverine. Electron microscopy revealed that defective PG-cadaverine decreased the structural interactions between peptidoglycan and the outer membrane, consistent with the proposed role for PG-cadaverine. The C-terminal β-strand-rich region of Mep45 was predicted to be a membrane-bound unit of the 14-stranded β-barrel structure. Here we propose that PG-cadaverine possesses functional importance to facilitate the structural linkage between peptidoglycan and the outer membrane via specific interaction with the SLH domain of Mep45.

Advanced approaches for the characterization of a de novo designed antiparallel coiled coil peptide

2005 ◽  
Vol 3 (7) ◽  
pp. 1189 ◽  
Author(s):  
Kevin Pagel ◽  
Karsten Seeger ◽  
Bettina Seiwert ◽  
Alessandra VillaCurrent address: J. W. Goethe ◽  
Alan E. Mark ◽  
...  
Keyword(s):  
De Novo ◽  
Coiled Coil ◽  
Antiparallel Coiled Coil

scholarly journals Structural basis of STAT2 recognition by IRF9 reveals molecular insights into ISGF3 function

2017 ◽  
Author(s):  
Srinivasan Rengachari ◽  
Silvia Groiss ◽  
Juliette Devos ◽  
Elise Caron ◽  
Nathalie Grandvaux ◽  
...  
Keyword(s):  
Cell Fate ◽  
Specific Interaction ◽  
Coiled Coil ◽  
Nuclear Gene ◽  
Type I Interferons ◽  
Structural Basis ◽  
Type I ◽  
Signalling Molecules ◽  
Nuclear Gene Expression ◽  
Selective Interaction

SummaryCytokine signalling is mediated by the activation of distinct sets of structurally homologous JAK and STAT signalling molecules, which control nuclear gene expression and cell fate. A significant expansion in the gene regulatory repertoire controlled by JAK/STAT signalling has arisen by the selective interaction of STATs with IRF transcription factors. Type I interferons (IFN), the major antiviral cytokines, trigger the formation of the ISGF3 complex containing STAT1, STAT2 and IRF9. ISGF3 regulates the expression of IFN–stimulated genes (ISGs). ISGF3 assembly depends on selective interaction between IRF9, through its IRF–association domain (IAD), with the coiled–coil domain (CCD) of STAT2. Here, we report the crystal structures of the IRF9–IAD alone and in a complex with STAT2–CCD. Despite similarity in the overall structure among respective paralogs, the surface features of the IRF9–IAD and STAT2– CCD have diverged to enable specific interaction between these family members, thus enabling ISGF3 formation and expression of ISGs.

scholarly journals Determination of the Multimerization State of the Hepatitis Delta Virus Antigens In Vivo

2003 ◽  
Vol 77 (19) ◽  
pp. 10314-10326 ◽  
Author(s):  
Cromwell T. Cornillez-Ty ◽  
David W. Lazinski
Keyword(s):  
Crystal Structure ◽  
Hepatitis Delta Virus ◽  
Coiled Coil ◽  
Proper Function ◽  
Hepatitis Delta ◽  
Amino Terminal ◽  
Delta Antigen ◽  
Antiparallel Coiled Coil ◽  
Delta Virus

ABSTRACT Hepatitis delta virus expresses two essential proteins, the small and large delta antigens, and both are required for viral propagation. Proper function of each protein depends on the presence of a common amino-terminal multimerization domain. A crystal structure, solved using a peptide fragment that contained residues 12 to 60, depicts the formation of an octameric ring composed of antiparallel coiled-coil dimers. Because this crystal structure was solved for only a fragment of the delta antigens, it is unknown whether octamers actually form in vivo at physiological protein concentrations and in the context of either intact delta antigen. To test the relevance of the octameric structure, we developed a new method to probe coiled-coil structures in vivo. We generated a panel of mutants containing cysteine substitutions at strategic locations within the predicted monomer-monomer interface and the dimer-dimer interface. Since the small delta antigen contains no cysteine residues, treatment of cell extracts with a mild oxidizing reagent was expected to induce disulfide bond formation only when the appropriate pairs of cysteine substitution mutants were coexpressed. We indeed found that, in vivo, both the small and large delta antigens assembled as antiparallel coiled-coil dimers. Likewise, we found that both proteins could assume an octameric quaternary structure in vivo. Finally, during the course of these experiments, we found that unprenylated large delta antigen molecules could be disulfide cross-linked via the sole cysteine residue located within the carboxy terminus. Therefore, in vivo, the C terminus likely provides an additional site of protein-protein interaction for the large delta antigen.

scholarly journals Molecular architecture of a dynamin adaptor: implications for assembly of mitochondrial fission complexes

2010 ◽  
Vol 191 (6) ◽  
pp. 1127-1139 ◽  
Author(s):  
Sajjan Koirala ◽  
Huyen T. Bui ◽  
Heidi L. Schubert ◽  
Debra M. Eckert ◽  
Christopher P. Hill ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Crystal Structures ◽  
Binding Sites ◽  
Mitochondrial Fission ◽  
Coiled Coil ◽  
Adaptor Proteins ◽  
Molecular Architecture ◽  
Cellular Membranes ◽  
Membrane Scission ◽  
Antiparallel Coiled Coil

Recruitment and assembly of some dynamin-related guanosine triphosphatases depends on adaptor proteins restricted to distinct cellular membranes. The yeast Mdv1 adaptor localizes to mitochondria by binding to the membrane protein Fis1. Subsequent Mdv1 binding to the mitochondrial dynamin Dnm1 stimulates Dnm1 assembly into spirals, which encircle and divide the mitochondrial compartment. In this study, we report that dimeric Mdv1 is joined at its center by a 92-Å antiparallel coiled coil (CC). Modeling of the Fis1–Mdv1 complex using available crystal structures suggests that the Mdv1 CC lies parallel to the bilayer with N termini at opposite ends bound to Fis1 and C-terminal β-propeller domains (Dnm1-binding sites) extending into the cytoplasm. A CC length of appropriate length and sequence is necessary for optimal Mdv1 interaction with Fis1 and Dnm1 and is important for proper Dnm1 assembly before membrane scission. Our results provide a framework for understanding how adaptors act as scaffolds to orient and stabilize the assembly of dynamins on membranes.

The Hyperthermophile Protein Sso10a is a Dimer of Winged Helix DNA-binding Domains Linked by an Antiparallel Coiled Coil Rod

2004 ◽  
Vol 341 (1) ◽  
pp. 73-91 ◽  
Author(s):  
Liqing Chen ◽  
Li-Rong Chen ◽  
Xiaoyin E. Zhou ◽  
Yujun Wang ◽  
Mebrahtu A. Kahsai ◽  
...  
Keyword(s):  
Dna Binding ◽  
Coiled Coil ◽  
Winged Helix ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Antiparallel Coiled Coil

Solution Structure of the C-terminal Antiparallel Coiled-coil Domain from Escherichia coli Osmosensor ProP

2003 ◽  
Vol 334 (5) ◽  
pp. 1063-1076 ◽  
Author(s):  
David L Zoetewey ◽  
Brian P Tripet ◽  
Tatiana G Kutateladze ◽  
Michael J Overduin ◽  
Janet M Wood ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Solution Structure ◽  
Coiled Coil ◽  
Coiled Coil Domain ◽  
Antiparallel Coiled Coil

scholarly journals Preferred side-chain constellations at antiparallel coiled-coil interfaces

2008 ◽  
Vol 105 (2) ◽  
pp. 530-535 ◽  
Author(s):  
E. B. Hadley ◽  
O. D. Testa ◽  
D. N. Woolfson ◽  
S. H. Gellman
Keyword(s):  
Coiled Coil ◽  
Side Chain ◽  
Antiparallel Coiled Coil
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