Crystallization and preliminary X-ray crystallographic analysis of Human Geminin Coiled-coil domain

2002 ◽  
Vol 1599 (1-2) ◽  
pp. 149-151 ◽  
Author(s):  
Michael Thépaut ◽  
François Hoh ◽  
Christian Dumas ◽  
Bernard Calas ◽  
Marie-Paule Strub ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Crystallographic Analysis ◽  
X Ray ◽  
Coiled Coil Domain

scholarly journals Over-Production, Crystallization, and Preliminary X-ray Crystallographic Analysis of a Coiled-Coil Region in Human Pericentrin

Crystals ◽  
2017 ◽  
Vol 7 (10) ◽  
pp. 296
Author(s):  
Min Kim ◽  
Jeong Park ◽  
Yeowon Sim ◽  
Doheum Kim ◽  
Jeong Sim ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Crystallographic Analysis ◽  
X Ray ◽  
Coiled Coil Region

scholarly journals X-ray crystallographic studies of the middle part of the human synaptonemal complex protein 1 coiled-coil domain

2015 ◽  
Vol 71 (9) ◽  
pp. 1131-1134 ◽  
Author(s):  
Hyun Ho Park
Keyword(s):  
Synaptonemal Complex ◽  
Short Form ◽  
Complex Structure ◽  
Coiled Coil ◽  
Middle Part ◽  
X Ray ◽  
Cell Parameters ◽  
Coiled Coil Domain ◽  
Complex Protein ◽  
Synaptonemal Complex Protein

The synaptonemal complex is a meiosis-specific complex structure formed at the synapse of homologous chromosomes to hold them together during meiosis. Synaptonemal complex protein 1 (SYCP1) is one of the components of the syneptonemal complex. In this study, the short form of the coiled-coil domain of SYCP1 was overexpressed inEscherichia coliwith an engineered C-terminal His tag. The short form of the coiled-coil domain of SYCP1 was then purified to homogeneity and crystallized at 293 K. X-ray diffraction data were collected to a resolution of 3.0 Å from a crystal belonging to space groupI4, with unit-cell parametersa= 41.95,b= 41.95,c= 318.78 Å. The asymmetric unit was estimated to contain two molecules.

scholarly journals Crystallization and preliminary X-ray crystallographic studies of the coiled-coil domain of PIST

2013 ◽  
Vol 69 (4) ◽  
pp. 468-471
Author(s):  
Young-Cheul Shin ◽  
Eun Kyoung Seo ◽  
Ju-Hong Jeon ◽  
Hyun Ho Park
Keyword(s):  
Escherichia Coli ◽  
Membrane Trafficking ◽  
Coiled Coil ◽  
Cancer Development ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
Coiled Coil Domain ◽  
Discs Large

PIST [PDZ (PSD-95, Discs-large and ZO-1) protein interacting specifically with TC10] functions as a regulator of membrane trafficking with Rab6A. Recently, the involvement of the fusion of PIST with ROS1 in cancer development has been identified. In this study, the coiled-coil domain of PIST, which is the domain responsible for interaction with Rab6A and fusion with ROS1, corresponding to amino acids 29–133, was overexpressed inEscherichia coliusing engineered C-terminal His tags. The coiled-coil domain of PIST was then purified to homogeneity and crystallized at 293 K. Finally, X-ray diffraction data were collected to a resolution of 4.0 Å from a crystal belonging to the hexagonal space groupP6222 orP6422, with unit-cell parametersa=b= 85.19,c= 240.09 Å, γ = 120.00°.

scholarly journals The coiled-coil domain of glycosomal membrane-associated Leishmania donovani PEX14: cloning, overexpression, purification and preliminary crystallographic analysis

2020 ◽  
Vol 76 (10) ◽  
pp. 464-468
Author(s):  
Anil Kumar Shakya ◽  
J. Venkatesh Pratap
Keyword(s):  
Leishmania Donovani ◽  
Protein Import ◽  
Transmembrane Domain ◽  
Coiled Coil ◽  
Supramolecular Assembly ◽  
Crystallographic Analysis ◽  
Size Exclusion ◽  
Monoclinic Space Group ◽  
Cell Parameters ◽  
Coiled Coil Domain

The glycosomal membrane-associated Leishmania donovani protein PEX14, which plays a crucial role in protein import from the cytosol to the glycosomal matrix, consists of three domains: an N-terminal domain where the signalling molecule binds, a transmembrane domain and an 84-residue coiled-coil domain (CC) that is responsible for oligomerization. CCs are versatile domains that participate in a variety of functions including supramolecular assembly, cellular signalling and transport. Recombinant PEX14 CC was cloned, overexpressed, affinity-purified with in-column thrombin cleavage and further purified by size-exclusion chromatography. Crystals that diffracted to 1.98 Å resolution were obtained from a condition consisting of 1.4 M sodium citrate tribasic dihydrate, 0.1 M HEPES buffer pH 7.5. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 143.98, b = 32.62, c = 95.62 Å, β = 94.68°. Structure determination and characterization are in progress.

Quaternary structure of Limulus polyphemus hemocyanin

1978 ◽  
Vol 36 (2) ◽  
pp. 176-177
Author(s):  
T. Wichertjes ◽  
E.J. Kwak ◽  
E.F.J. Van Bruggen
Keyword(s):  
Electron Microscopy ◽  
Functional Properties ◽  
Horseshoe Crab ◽  
Temperature Jump ◽  
Quaternary Structure ◽  
Crystallographic Analysis ◽  
Limulus Polyphemus ◽  
Oxygen Binding ◽  
X Ray ◽  
Intact Molecule

Hemocyanin of the horseshoe crab (Limulus polyphemus) has been studied in nany ways. Recently the structure, dissociation and reassembly was studied using electron microscopy of negatively stained specimens as the method of investigation. Crystallization of the protein proved to be possible and X-ray crystallographic analysis was started. Also fluorescence properties of the hemocyanin after dialysis against Tris-glycine buffer + 0.01 M EDTA pH 8.9 (so called “stripped” hemocyanin) and its fractions II and V were studied, as well as functional properties of the fractions by NMR. Finally the temperature-jump method was used for assaying the oxygen binding of the dissociating molecule and of preparations of isolated subunits. Nevertheless very little is known about the structure of the intact molecule. Schutter et al. suggested that the molecule possibly consists of two halves, combined in a staggered way, the halves themselves consisting of four subunits arranged in a square.

TMCC3 localizes at the three-way junctions for the proper tubular network of the endoplasmic reticulum

2019 ◽  
Vol 476 (21) ◽  
pp. 3241-3260
Author(s):  
Sindhu Wisesa ◽  
Yasunori Yamamoto ◽  
Toshiaki Sakisaka
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Mammalian Cells ◽  
Coiled Coil ◽  
Transmembrane Domains ◽  
Domain Family ◽  
Coiled Coil Domain ◽  
U2os Cells ◽  
Er Membrane

The tubular network of the endoplasmic reticulum (ER) is formed by connecting ER tubules through three-way junctions. Two classes of the conserved ER membrane proteins, atlastins and lunapark, have been shown to reside at the three-way junctions so far and be involved in the generation and stabilization of the three-way junctions. In this study, we report TMCC3 (transmembrane and coiled-coil domain family 3), a member of the TEX28 family, as another ER membrane protein that resides at the three-way junctions in mammalian cells. When the TEX28 family members were transfected into U2OS cells, TMCC3 specifically localized at the three-way junctions in the peripheral ER. TMCC3 bound to atlastins through the C-terminal transmembrane domains. A TMCC3 mutant lacking the N-terminal coiled-coil domain abolished localization to the three-way junctions, suggesting that TMCC3 localized independently of binding to atlastins. TMCC3 knockdown caused a decrease in the number of three-way junctions and expansion of ER sheets, leading to a reduction of the tubular ER network in U2OS cells. The TMCC3 knockdown phenotype was partially rescued by the overexpression of atlastin-2, suggesting that TMCC3 knockdown would decrease the activity of atlastins. These results indicate that TMCC3 localizes at the three-way junctions for the proper tubular ER network.

Sign in / Sign up

Export Citation Format

Share Document