- Structural insights into the psychrophilic germinal protease PaGPR and its autoinhibitory loop
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Chang Woo Lee , Saeyoung Lee , Chang-Sook Jeong , Jisub Hwang , Jeong Ho Chang , In-Geol Choi , T. Doohun Kim , HaJeung Park , Hye-Yeon Kim , Jun Hyuck Lee
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J. Microbiol. 2020;58(9):772-779. Published online September 1, 2020
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DOI: https://doi.org/10.1007/s12275-020-0292-0
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 Abstract
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In spore forming microbes, germination protease (GPR) plays
a key role in the initiation of the germination process. A critical
step during germination is the degradation of small acidsoluble
proteins (SASPs), which protect spore DNA from external
stresses (UV, heat, low temperature, etc.). Inactive zymogen
GPR can be activated by autoprocessing of the N-terminal
pro-sequence domain. Activated GPR initiates the degradation
of SASPs; however, the detailed mechanisms underlying
the activation, catalysis, regulation, and substrate
recognition of GPR remain elusive. In this study, we determined
the crystal structure of GPR from Paenisporosarcina
sp. TG-20 (PaGPR) in its inactive form at a resolution of 2.5
Å. Structural analysis showed that the active site of PaGPR
is sterically occluded by an inhibitory loop region (residues
202–216). The N-terminal region interacts directly with the
self-inhibitory loop region, suggesting that the removal of the
N-terminal pro-sequence induces conformational changes,
which lead to the release of the self-inhibitory loop region
from the active site. In addition, comparative sequence and
structural analyses revealed that PaGPR contains two highly
conserved Asp residues (D123 and D182) in the active site,
similar to the putative aspartic acid protease GPR from Bacillus
megaterium. The catalytic domain structure of PaGPR
also shares similarities with the sequentially non-homologous
proteins HycI and HybD. HycI and HybD are metalloproteases
that also contain two Asp (or Glu) residues in their
active site, playing a role in metal binding. In summary, our
results
provide useful insights into the activation process of
PaGPR and its active conformation.
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Citations
Citations to this article as recorded by  - Crystal structure of human LC8 bound to a peptide from Ebola virus VP35
Dahwan Lim, Ho-Chul Shin, Joon Sig Choi, Seung Jun Kim, Bonsu Ku
Journal of Microbiology.2021; 59(4): 410. CrossRef - Purification and Crystallographic Analysis of a Novel Cold-Active Esterase (HaEst1) from Halocynthiibacter arcticus
Sangeun Jeon, Jisub Hwang, Wanki Yoo, Joo Won Chang, Hackwon Do, Han-Woo Kim, Kyeong Kyu Kim, Jun Hyuck Lee, T. Doohun Kim
Crystals.2021; 11(2): 170. CrossRef
- Crystal structure of the bacterial type VI secretion system component TssL from Vibrio cholerae
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Jeong Ho Chang , Yeon-Gil Kim
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J. Microbiol. 2015;53(1):32-37. Published online December 4, 2014
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DOI: https://doi.org/10.1007/s12275-015-4539-0
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927
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Abstract
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The type VI secretion system (T6SS), commonly found in
Gram-negative bacteria, is responsible for exporting effector
proteins. The T6SS has been reported to be cytotoxic to host
cells. While the components and assembly of the T6SS complex
have been largely assessed, structural data on T6SS components
from virulent bacteria is remarkably insufficient.
Here, we report the crystal structure of Vibrio cholerae TssL
(VcTssL), a core component of T6SS. In spite of a relatively
low sequence identity, the overall structure of VcTssL is largely
similar to those from other bacterial homologs except
for several differences found in local structural elements. A
unique feature attributed to the C-terminal fragment of Vc-
TssL is a crystallographic artifact. This incidental feature of
VcTssL may provide insights into screening of molecular
partners for the cytoplasmic domain of TssL. Additionally,
our results may help in the design of molecular probes for a
detailed understanding of the functional relationship between
TssL and other T6SS components.
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Citations
Citations to this article as recorded by - Structural Characterization of TssL from Acinetobacter baumannii: a Key Component of the Type VI Secretion System
Federico M. Ruiz, Juvenal Lopez, C. Gastón Ferrara, Elena Santillana, Yanis R. Espinosa, Mario F. Feldman, Antonio Romero, Ann M. Stock
Journal of Bacteriology.2020;[Epub] CrossRef - In situ and high‐resolution cryo‐EM structure of a bacterial type VI secretion system membrane complex
Chiara Rapisarda, Yassine Cherrak, Romain Kooger, Victoria Schmidt, Riccardo Pellarin, Laureen Logger, Eric Cascales, Martin Pilhofer, Eric Durand, Rémi Fronzes
The EMBO Journal.2019;[Epub] CrossRef - Crystal Structure of the Type VI Secretion System Accessory Protein TagF from Pseudomonas Aeruginosa
Chang-Kyu Ok, Jeong Ho Chang
Protein & Peptide Letters.2019; 26(3): 204. CrossRef - Structure and Activity of the Type VI Secretion System
Yassine Cherrak, Nicolas Flaugnatti, Eric Durand, Laure Journet, Eric Cascales, Maria Sandkvist, Peter J. Christie
Microbiology Spectrum.2019;[Epub] CrossRef - Crystal structure of the periplasmic domain of TssL, a key membrane component of Type VI secretion system
Xiangbei Wang, Bo Sun, Mengxue Xu, Shenshen Qiu, Dongqing Xu, Tingting Ran, Jianhua He, Weiwu Wang
International Journal of Biological Macromolecules.2018; 120: 1474. CrossRef - Tryptophan-mediated Dimerization of the TssL Transmembrane Anchor Is Required for Type VI Secretion System Activity
Abdelrahim Zoued, Jean-Pierre Duneau, Eric Durand, Alexandre P. España, Laure Journet, Françoise Guerlesquin, Eric Cascales
Journal of Molecular Biology.2018; 430(7): 987. CrossRef - Structure–Function Analysis of the TssL Cytoplasmic Domain Reveals a New Interaction between the Type VI Secretion Baseplate and Membrane Complexes
Abdelrahim Zoued, Chloé J. Cassaro, Eric Durand, Badreddine Douzi, Alexandre P. España, Christian Cambillau, Laure Journet, Eric Cascales
Journal of Molecular Biology.2016; 428(22): 4413. CrossRef - Aim, Load, Fire: The Type VI Secretion System, a Bacterial Nanoweapon
Francesca R. Cianfanelli, Laura Monlezun, Sarah J. Coulthurst
Trends in Microbiology.2016; 24(1): 51. CrossRef - Biogenesis and structure of a type VI secretion membrane core complex
Eric Durand, Van Son Nguyen, Abdelrahim Zoued, Laureen Logger, Gérard Péhau-Arnaudet, Marie-Stéphanie Aschtgen, Silvia Spinelli, Aline Desmyter, Benjamin Bardiaux, Annick Dujeancourt, Alain Roussel, Christian Cambillau, Eric Cascales, Rémi Fronzes
Nature.2015; 523(7562): 555. CrossRef - Type VI secretion system: secretion by a contractile nanomachine
Marek Basler
Philosophical Transactions of the Royal Society B: Biological Sciences.2015; 370(1679): 20150021. CrossRef
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