The C-terminal domain conformational switch revealed by the crystal structure of malyl-CoA lyase from Roseiflexus castenholzii

2019 ◽  
Vol 518 (1) ◽  
pp. 72-79
Author(s):  
Wanrong Tang ◽  
Zhiguo Wang ◽  
Chenyun Zhang ◽  
Chao Wang ◽  
Zhenzhen Min ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Conformational Switch ◽  
Terminal Domain

scholarly journals Author Correction: Crystal structure of Type IX secretion system PorE C-terminal domain from Porphyromonas gingivalis in complex with a peptidoglycan fragment

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Nhung Thi Trang Trinh ◽  
Hieu Quang Tran ◽  
Quyen Van Dong ◽  
Christian Cambillau ◽  
Alain Roussel ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Porphyromonas Gingivalis ◽  
Secretion System ◽  
Terminal Domain ◽  
Type Ix Secretion System

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

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 Crystal structure of the N-terminal domain of VqsR fromPseudomonas aeruginosaat 2.1 Å resolution

2017 ◽  
Vol 73 (7) ◽  
pp. 431-436
Author(s):  
Qing He ◽  
Kang Wang ◽  
Tiantian Su ◽  
Feng Wang ◽  
Lichuan Gu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Sequence Similarity ◽  
Transcriptional Regulator ◽  
Binding Domain ◽  
Structural Comparison ◽  
Homoserine Lactones ◽  
Terminal Domain ◽  
C Terminus ◽  
Common Motif ◽  
The Common

VqsR is a quorum-sensing (QS) transcriptional regulator which controls QS systems (las,rhlandpqs) by directly downregulating the expression ofqscRinPseudomonas aeruginosa. As a member of the LuxR family of proteins, VqsR shares the common motif of a helix–turn–helix (HTH)-type DNA-binding domain at the C-terminus, while the function of its N-terminal domain remains obscure. Here, the crystal structure of the N-terminal domain of VqsR (VqsR-N; residues 1–193) was determined at a resolution of 2.1 Å. The structure is folded into a regular α–β–α sandwich topology, which is similar to the ligand-binding domain (LBD) of the LuxR-type QS receptors. Although their sequence similarity is very low, structural comparison reveals that VqsR-N has a conserved enclosed cavity which could recognize acyl-homoserine lactones (AHLs) as in other LuxR-type AHL receptors. The structure suggests that VqsR could be a potential AHL receptor.

The 1.8-Å Crystal Structure of the N-Terminal Domain of an Archaeal MCM as a Right-Handed Filament

2014 ◽  
Vol 426 (7) ◽  
pp. 1512-1523 ◽  
Author(s):  
Yang Fu ◽  
Ian M. Slaymaker ◽  
Junfeng Wang ◽  
Ganggang Wang ◽  
Xiaojiang S. Chen
Keyword(s):  
Crystal Structure ◽  
Terminal Domain

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

10.3791/58568 ◽  
2018 ◽  
Author(s):  
Bidhan Chandra Nayak ◽  
Jie Wang ◽  
Lianyun Lin ◽  
Weiyi He ◽  
Minsheng You ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ryanodine Receptor ◽  
Plutella Xylostella ◽  
Terminal Domain

scholarly journals Crystal Structure and Trimer-Monomer Transition of N-Terminal Domain of EhCaBP1 from Entamoeba histolytica

2010 ◽  
Vol 98 (12) ◽  
pp. 2933-2942 ◽  
Author(s):  
Shivesh Kumar ◽  
Ejaz Ahmad ◽  
M. Shahid Mansuri ◽  
Sanjeev Kumar ◽  
Ruchi Jain ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Entamoeba Histolytica ◽  
Terminal Domain

scholarly journals Structural and biochemical characterization of bifunctional XynA

2020 ◽  
Author(s):  
Wei Xie ◽  
Qi Yu ◽  
Yun Liu ◽  
Ruoting Cao ◽  
Ruiqing Zhang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Enzyme Activity ◽  
Catalytic Mechanism ◽  
Biochemical Characterization ◽  
Cellulase Activity ◽  
Cost Savings ◽  
Site Directed Mutagenesis ◽  
Enzyme Activity Assay ◽  
Great Cost ◽  
Terminal Domain

AbstractXylan and cellulose are the two major constituents in numerous types of lignocellulosic biomass, representing a promising resource for biofuels and other biobased industries. The efficient degradation of lignocellulose requires the synergistic actions of cellulase and xylanase. Thus, bifunctional enzyme incorporated xylanase/cellulase activity has attracted considerable attention since it has great cost savings potential. Recently, a novel GH10 family enzyme XynA identified from Bacillus sp. is found to degrade both cellulose and xylan. To understand its molecular catalytic mechanism, here we first solve the crystal structure of XynA at 2.3 Å. XynA is characterized with a classic (α/β)8 TIM-barrel fold (GH10 domain) flanked by the flexible N-terminal domain and C-terminal domain. Circular dichroism, protein thermal shift and enzyme activity assays reveal that conserved residues Glu182 and Glu280 are both important for catalytic activities of XynA, which is verified by the crystal structure of XynA with E182A/E280A double mutant. Molecular docking studies of XynA with xylohexaose and cellohexaose as well as site-directed mutagenesis and enzyme activity assay demonstrat that Gln250 and His252 are indispensible to cellulase and bifunctional activity, separately. These results elucidate the structural and biochemical features of XynA, providing clues for further modification of XynA for industrial application.

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