scholarly journals Crystal structure of calcium-free human sorcin: A member of the penta-EF-hand protein family

2008 ◽  
Vol 10 (12) ◽  
pp. 2419-2425 ◽  
Author(s):  
Xiaoling Xie ◽  
Maureen D. Dwyer ◽  
Lora Swenson ◽  
Matthew H. Parker ◽  
Martyn C. Botfield
Keyword(s):  
Crystal Structure ◽  
Protein Family ◽  
Ef Hand

scholarly journals Crystal structures of Ca2+–calmodulin bound to NaV C-terminal regions suggest role for EF-hand domain in binding and inactivation

2019 ◽  
Vol 116 (22) ◽  
pp. 10763-10772 ◽  
Author(s):  
Bernd R. Gardill ◽  
Ricardo E. Rivera-Acevedo ◽  
Ching-Chieh Tung ◽  
Filip Van Petegem
Keyword(s):  
Crystal Structure ◽  
Binding Sites ◽  
Binding Mode ◽  
Conformational Switch ◽  
Channel Inactivation ◽  
Dependent Inactivation ◽  
Ef Hand ◽  
Inherited Arrhythmia ◽  
A Site

Voltage-gated sodium (NaV) and calcium channels (CaV) form targets for calmodulin (CaM), which affects channel inactivation properties. A major interaction site for CaM resides in the C-terminal (CT) region, consisting of an IQ domain downstream of an EF-hand domain. We present a crystal structure of fully Ca2+-occupied CaM, bound to the CT of NaV1.5. The structure shows that the C-terminal lobe binds to a site ∼90° rotated relative to a previous site reported for an apoCaM complex with the NaV1.5 CT and for ternary complexes containing fibroblast growth factor homologous factors (FHF). We show that the binding of FHFs forces the EF-hand domain in a conformation that does not allow binding of the Ca2+-occupied C-lobe of CaM. These observations highlight the central role of the EF-hand domain in modulating the binding mode of CaM. The binding sites for Ca2+-free and Ca2+-occupied CaM contain targets for mutations linked to long-QT syndrome, a type of inherited arrhythmia. The related NaV1.4 channel has been shown to undergo Ca2+-dependent inactivation (CDI) akin to CaVs. We present a crystal structure of Ca2+/CaM bound to the NaV1.4 IQ domain, which shows a binding mode that would clash with the EF-hand domain. We postulate the relative reorientation of the EF-hand domain and the IQ domain as a possible conformational switch that underlies CDI.

scholarly journals The crystal structure of amyloid precursor‐like protein 2 E2 domain completes the amyloid precursor protein family

2019 ◽  
Vol 33 (4) ◽  
pp. 5076-5081 ◽  
Author(s):  
Laila C. Roisman ◽  
Sen Han ◽  
Mun Joo Chuei ◽  
Andrea R. Connor ◽  
Roberto Cappai
Keyword(s):  
Crystal Structure ◽  
Amyloid Precursor Protein ◽  
Protein Family ◽  
Precursor Protein

scholarly journals The crystal structure of Arabidopsis BON1 provides insights into the copine protein family

2020 ◽  
Vol 103 (3) ◽  
pp. 1215-1232 ◽  
Author(s):  
Qianchao Wang ◽  
Meiqin Jiang ◽  
Michail N. Isupov ◽  
Yayu Chen ◽  
Jennifer A. Littlechild ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Protein Family

scholarly journals The Sec1p/Munc18 protein Vps45p binds its cognate SNARE proteins via two distinct modes

2006 ◽  
Vol 173 (6) ◽  
pp. 927-936 ◽  
Author(s):  
Lindsay N. Carpp ◽  
Leonora F. Ciufo ◽  
Scott G. Shanks ◽  
Alan Boyd ◽  
Nia J. Bryant
Keyword(s):  
Crystal Structure ◽  
Membrane Trafficking ◽  
Protein Family ◽  
Snare Proteins ◽  
Outer Face ◽  
Sm Proteins ◽  
Hydrophobic Pocket ◽  
Second Mode ◽  
Sm Protein ◽  
Domain I

Sec1p/Munc18 (SM) proteins are essential for SNARE-mediated membrane trafficking. The formulation of unifying hypotheses for the function of the SM protein family has been hampered by the observation that two of its members bind their cognate syntaxins (Sxs) in strikingly different ways. The SM protein Vps45p binds its Sx Tlg2p in a manner analogous to that captured by the Sly1p–Sed5p crystal structure, whereby the NH2-terminal peptide of the Sx inserts into a hydrophobic pocket on the outer face of domain I of the SM protein. In this study, we report that although this mode of interaction is critical for the binding of Vps45p to Tlg2p, the SM protein also binds Tlg2p-containing SNARE complexes via a second mode that involves neither the NH2 terminus of Tlg2p nor the region of Vps45p that facilitates this interaction. Our findings point to the possibility that SM proteins interact with their cognate SNARE proteins through distinct mechanisms at different stages in the SNARE assembly/disassembly cycle.

scholarly journals Crystal structure and calcium‐induced conformational changes of diacylglycerol kinase α EF‐hand domains

2019 ◽  
Vol 28 (4) ◽  
pp. 694-706 ◽  
Author(s):  
Daisuke Takahashi ◽  
Kano Suzuki ◽  
Taiichi Sakamoto ◽  
Takeo Iwamoto ◽  
Takeshi Murata ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Conformational Changes ◽  
Diacylglycerol Kinase ◽  
Ef Hand

scholarly journals Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand

Structure ◽  
1999 ◽  
Vol 7 (10) ◽  
pp. 1167-1180 ◽  
Author(s):  
Erik J van Asselt ◽  
Arnoud J Dijkstra ◽  
Kor H Kalk ◽  
Bela Takacs ◽  
Wolfgang Keck ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Catalytic Domain ◽  
Lytic Transglycosylase ◽  
Ef Hand

scholarly journals Reconstruction of Mycobacterial Dehalogenase Rv2579 by Cumulative Mutagenesis of Haloalkane Dehalogenase LinB

2003 ◽  
Vol 69 (4) ◽  
pp. 2349-2355 ◽  
Author(s):  
Yuji Nagata ◽  
Zbyněk Prokop ◽  
Soňa Marvanová ◽  
Jana Sýkorová ◽  
Marta Monincová ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Mycobacterium Tuberculosis ◽  
Amino Acid ◽  
Active Site ◽  
Homology Model ◽  
Protein Family ◽  
Sphingomonas Paucimobilis ◽  
Amino Acid Residues ◽  
Haloalkane Dehalogenase

ABSTRACT The homology model of protein Rv2579 from Mycobacterium tuberculosis H37Rv was compared with the crystal structure of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26, and this analysis revealed that 6 of 19 amino acid residues which form an active site and entrance tunnel are different in LinB and Rv2579. To characterize the effect of replacement of these six amino acid residues, mutations were introduced cumulatively into the six amino acid residues of LinB. The sixfold mutant, which was supposed to have the active site of Rv2579, exhibited haloalkane dehalogenase activity with the haloalkanes tested, confirming that Rv2579 is a member of the haloalkane dehalogenase protein family.

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