X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil

Science ◽  
1991 ◽  
Vol 254 (5031) ◽  
pp. 539-544 ◽  
Author(s):  
E. O'Shea ◽  
J. Klemm ◽  
P. Kim ◽  
T Alber
Keyword(s):  
Leucine Zipper ◽  
Coiled Coil ◽  
X Ray

scholarly journals X-ray scattering indicates that the leucine zipper is a coiled coil.

1991 ◽  
Vol 88 (2) ◽  
pp. 561-564 ◽  
Author(s):  
R. Rasmussen ◽  
D. Benvegnu ◽  
E. K. O'Shea ◽  
P. S. Kim ◽  
T. Alber
Keyword(s):  
Leucine Zipper ◽  
Coiled Coil ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

Leucine Is the Most Stabilizing Aliphatic Amino Acid in thedPosition of a Dimeric Leucine Zipper Coiled Coil

Biochemistry ◽  
1997 ◽  
Vol 36 (41) ◽  
pp. 12567-12573 ◽  
Author(s):  
Jaideep Moitra ◽  
Lászlo Szilák ◽  
Dmitry Krylov ◽  
Charles Vinson
Keyword(s):  
Amino Acid ◽  
Leucine Zipper ◽  
Coiled Coil ◽  
Aliphatic Amino Acid

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

New Approach to Detect Coiled Coil and Leucine Zipper Motifs in Protein Sequences

2018 ◽  
Vol 25 (11) ◽  
pp. 1278-1283
Author(s):  
Dinko Osmankovic ◽  
Semir Doric ◽  
Naris Pojskic ◽  
Lada Lukic Bilela
Keyword(s):  
Leucine Zipper ◽  
Coiled Coil ◽  
Protein Sequences ◽  
New Approach

scholarly journals Structural basis for the coiled-coil architecture of human CtIP

2021 ◽  
Author(s):  
C. R. Morton ◽  
N. J. Rzechorzek ◽  
J. D. Maman ◽  
M. Kuramochi ◽  
H. Sekiguchi ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Three Dimensional ◽  
Coiled Coil ◽  
Strand Break ◽  
Structural Basis ◽  
Binding Motif ◽  
Chromosomal Dna ◽  
Dsb Repair ◽  
Critical Function ◽  
X Ray

AbstractThe DNA repair factor CtIP has a critical function in Double-Strand Break (DSB) repair by Homologous Recombination, promoting the assembly of the repair apparatus at DNA ends and participating in DNA-end resection. However, the molecular mechanisms of CtIP function in DSB repair remain unclear. Here we present an atomic model for the three-dimensional architecture of human CtIP, derived from a multi-disciplinary approach that includes X-ray crystallography, Small-angle X-ray Scattering (SAXS) and Diffracted X-ray Tracking (DXT). Our data show that CtIP adopts an extended dimer-of-dimers structure, in agreement with a role in bridging distant sites on chromosomal DNA during recombinational repair. The zinc-binding motif in CtIP’s N-terminus alters dynamically the coiled coil structure, with functional implications for the long-range interactions of CtIP with DNA. Our results provide a structural basis for the three-dimensional arrangement of chains in the CtIP tetramer, a key aspect of CtIP function in DNA DSB repair.

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 Evidence for an Elongated Dimeric Structure of Heparin-Binding Hemagglutinin from Mycobacterium tuberculosis

2008 ◽  
Vol 190 (13) ◽  
pp. 4749-4753 ◽  
Author(s):  
Carla Esposito ◽  
Maxim V. Pethoukov ◽  
Dmitri I. Svergun ◽  
Alessia Ruggiero ◽  
Carlo Pedone ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Virulence Factor ◽  
Biochemical Characterization ◽  
Coiled Coil ◽  
Heparin Binding ◽  
Truncated Form ◽  
X Ray ◽  
Dimeric Structure ◽  
X Ray Scattering

ABSTRACT Heparin-binding hemagglutinin (HBHA) is a virulence factor of tuberculosis which is responsible for extrapulmonary dissemination of this disease. A thorough biochemical characterization of HBHA has provided experimental evidence of a coiled-coil nature of HBHA. These data, together with the low-resolution structures of a full-length form and a truncated form of HBHA obtained by small-angle X-ray scattering, have unambiguously indicated that HBHA has a dimeric structure with an elongated shape.

scholarly journals Image Reconstructions of Microtubules Decorated with Monomeric and Dimeric Kinesins: Comparison with X-Ray Structure and Implications for Motility

1998 ◽  
Vol 141 (2) ◽  
pp. 419-430 ◽  
Author(s):  
A. Hoenger ◽  
S. Sack ◽  
M. Thormählen ◽  
A. Marx ◽  
J. Müller ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Image Reconstruction ◽  
Three Dimensional ◽  
Coiled Coil ◽  
Cryoelectron Microscopy ◽  
Short Neck ◽  
X Ray ◽  
Dimensional Image ◽  
Tubulin Subunit ◽  
Image Reconstructions

We have decorated microtubules with monomeric and dimeric kinesin constructs, studied their structure by cryoelectron microscopy and three-dimensional image reconstruction, and compared the results with the x-ray crystal structure of monomeric and dimeric kinesin. A monomeric kinesin construct (rK354, containing only a short neck helix insufficient for coiled-coil formation) decorates microtubules with a stoichiometry of one kinesin head per tubulin subunit (α–β-heterodimer). The orientation of the kinesin head (an anterograde motor) on the microtubule surface is similar to that of ncd (a retrograde motor). A longer kinesin construct (rK379) forms a dimer because of the longer neck helix forming a coiled-coil. Unexpectedly, this construct also decorates the microtubule with a stoichiometry of one head per tubulin subunit, and the orientation is similar to that of the monomeric construct. This means that the interaction with microtubules causes the two heads of a kinesin dimer to separate sufficiently so that they can bind to two different tubulin subunits. This result is in contrast to recent models and can be explained by assuming that the tubulin–kinesin interaction is antagonistic to the coiled-coil interaction within a kinesin dimer.

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