scholarly journals Crystal structure of a super leucine zipper, an extended two-stranded super long coiled coil

2010 ◽  
Vol 19 (2) ◽  
pp. 319-326 ◽  
Author(s):  
Jiasheng Diao
Keyword(s):  
Crystal Structure ◽  
Leucine Zipper ◽  
Coiled Coil

scholarly journals Structure of a truncated form of leucine zipper II of JIP3 reveals an unexpected antiparallel coiled-coil arrangement

2016 ◽  
Vol 72 (3) ◽  
pp. 198-206 ◽  
Author(s):  
Paola Llinas ◽  
Mélanie Chenon ◽  
T. Quyen Nguyen ◽  
Catia Moreira ◽  
Annélie de Régibus ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Molecular Motors ◽  
Map Kinases ◽  
Leucine Zipper ◽  
Coiled Coil ◽  
Structural Rearrangement ◽  
Structural Motif ◽  
Scaffolding Proteins ◽  
Truncated Form ◽  
The Stability

JIP3 and JIP4, two highly related scaffolding proteins for MAP kinases, are binding partners for two molecular motors as well as for the small G protein ARF6. The leucine zipper II (LZII) region of JIP3/4 is the binding site for these three partners. Previously, the crystal structure of ARF6 bound to JIP4 revealed LZII in a parallel coiled-coil arrangement. Here, the crystal structure of an N-terminally truncated form of LZII of JIP3 alone shows an unexpected antiparallel arrangement. Using molecular dynamics and modelling, the stability of this antiparallel LZII arrangement, as well as its specificity for ARF6, were investigated. This study highlights that N-terminal truncation of LZII can change its coiled-coil orientation without affecting its overall stability. Further, a conserved buried asparagine residue was pinpointed as a possible structural determinant for this dramatic structural rearrangement. Thus, LZII of JIP3/4 is a versatile structural motif, modifications of which can impact partner recognition and thus biological function.

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

Crystal structure of an Lrs14-like archaeal biofilm regulator fromSulfolobus acidocaldarius

2018 ◽  
Vol 74 (11) ◽  
pp. 1105-1114
Author(s):  
Marian S. Vogt ◽  
Simon L. Völpel ◽  
Sonja-Verena Albers ◽  
Lars-Oliver Essen ◽  
Ankan Banerjee
Keyword(s):  
Crystal Structure ◽  
Biofilm Formation ◽  
Coiled Coil ◽  
Transcriptional Regulators ◽  
Bioinformatic Analysis ◽  
Considerable Degree ◽  
Sulfolobus Acidocaldarius ◽  
Asymmetric Unit ◽  
Winged Helix ◽  
Structural Differences

The small winged helix–turn–helix (wHTH) proteins of the Lrs14 family are major transcriptional regulators and act as archaeal biofilm regulators (AbfRs) in the crenarchaeoteSulfolobus acidocaldarius. Here, the first crystal structure of an AbfR ortholog, AbfR2, the deletion of which is known to impair biofilm formation, is presented. Like most other wHTH orthologs, AbfR2 is dimeric in solution as well as in its 2.45 Å resolution crystal structure. Given the presence of three independent AbfR2 dimers in the asymmetric unit, the crystal structure shows a considerable degree of conformational variation within the dimer, the antiparallel orientations of which are stabilized by coiled-coil interaction between H4 helices. Conserved anchor interactions between helices H0 and H4 of AbfR2 further contribute to dimer stabilization. The combined structural and bioinformatic analysis reveals cluster-specific structural differences between different members of the Lrs14 protein family.

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

Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues

1998 ◽  
Vol 284 (4) ◽  
pp. 859-865 ◽  
Author(s):  
Debra M Eckert ◽  
Vladimir N Malashkevich ◽  
Peter S Kim
Keyword(s):  
Crystal Structure ◽  
Coiled Coil ◽  
Polar Residues

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.

scholarly journals Crystal Structure of Mitochondrial Fission Complex Reveals Scaffolding Function for Mitochondrial Division 1 (Mdv1) Coiled Coil

2012 ◽  
Vol 287 (13) ◽  
pp. 9855-9861 ◽  
Author(s):  
Yan Zhang ◽  
Nickie C. Chan ◽  
Huu B. Ngo ◽  
Harry Gristick ◽  
David C. Chan
Keyword(s):  
Crystal Structure ◽  
Mitochondrial Fission ◽  
Coiled Coil ◽  
Mitochondrial Division ◽  
Division 1
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