自引率: 2.6%
被引量: 7900
通过率: 暂无数据
审稿周期: 1
版面费用: 暂无数据
国人发稿量: 13
投稿须知/期刊简介:
Published by Elsevier Science. ISSN: 1570-9639.<br /><br />One of the nine topical sections of Biochimica et Biophysica Acta. International Journal of Biochemistry, Biophysics and Molecular Biology. Former title: BBA - Protein Structure and Molecular Enzymology. BBA's Proteins and Proteomics section covers protein structure conformation and dynamics, protein-ligand interactions, enzyme mechanisms, models and kinetics, physical properties and spectroscopy. This section also includes Short crystallization papers describing the crystallization of proteins. Concise and comprehensive reviews of recent developments are considered for publication. However, authors are strongly advised to consult one of the Executive Editors before starting a review.
期刊描述简介:
BBA Proteins and Proteomics covers protein structure conformation and dynamics; protein folding; protein-ligand interactions; enzyme mechanisms, models and kinetics; protein physical properties and spectroscopy; and proteomics and bioinformatics analyses of protein structure, protein function, or protein regulation. Concise and comprehensive reviews of recent developments are considered for publication. However, authors are strongly advised to consult one of the Executive Editors before starting a review. Types of papers published: regular papers, reviews and mini-reviews.
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Serratiopeptidase exhibits antibiofilm activity through the proteolytic function of N-terminal domain and versatile function of the C-terminal domain.
Serratiopeptidase, a serine protease traditionally used as an oral anti-inflammatory drug has been found to show antibiofilm action. Structurally, it comprises of two distinct domains; viz-the N-terminal catalytic domain (Ncat) and a C-terminal RTX (Repeat-In-Toxin) domain (Crtx). Understanding the antibiofilm action of the serratiopeptidase molecule, as well as the antibiofilm action of each of its two domains, was the objective of this study. Separate clones to express the complete recombinant serratiopeptidase protein and its variant containing a mutation in the catalytic site, the N-terminal catalytic domain and its mutant, and the C-terminal Repeat-In-Toxin domain were prepared, and the proteins were purified. The impact of these proteins on pre-existing biofilms, as well as their effect upon addition of these proteins during biofilm formation was investigated. In our investigation, we have been able to analyze the antibiofilm action of serratiopeptidase in detail. Obtained results conclude that while N-terminally located proteolytic domain of serratiopeptidase conventionally acts against biofilms by hydrolytic activity, the C-terminal domain regulates or prevents biofilm formation by yet unknown mechanism in addition to its known function as an C-terminal located calcium modulated internal chaperone ensuring the proper folding and secretion of the molecule. The study's findings give new evidence that the Crtx domain plays a significant role in antibiofilm action. The proteolytic Ncat domain breaks down pre-formed biofilms. The C-terminal domain, on the other hand, acts as an inhibitor of biofilm formation by regulating or preventing biofilm development.
被引量：- 发表：1970
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From sequence to function: Exploring biophysical properties of bacteriophage BFK20 lytic transglycosylase domain from the minor tail protein gp15.
Bacteriophages have evolved different mechanisms of infection and penetration of bacterial cell walls. In Siphoviridae-like viruses, the inner tail proteins have a pivotal role in these processes and often encode lytic protein domains which increase infection efficiency. A soluble lytic transglycosylase (SLT) domain was identified in the minor tail protein gp15 from the BFK20 bacteriophage. Six fragments containing this SLT domain with adjacent regions of different lengths were cloned, expressed and purified. The biophysical properties of the two best expressing fragments were characterized by nanoDSF and CD spectroscopy, which showed that both fragments had a high refolding ability of 90 %. 3D modeling indicated that the bacteriophage BFK20 SLT domain is structurally similar to lysozyme. The degradation activity of these SLT proteins was evaluated using a lysozyme activity assay. BFK20 might use its transglycosylase activity to allow efficient phage DNA entry into the host cell by degrading bacterial peptidoglycan.
被引量：- 发表：1970
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Identification of potential pharmacological chaperones that selectively stabilize mutated Aspartoacylases in Canavan disease.
Canavan disease is caused by mutations in the ASPA gene, leading to diminished catalytic activity of aspartoacylase in the brain. Clinical missense mutations are found throughout the enzyme structure, with many of these mutated enzymes having not only decreased activity but also compromised stability. High-throughput screening of a small molecule library has identified several compounds that significantly increase the thermal stability of the E285A mutant enzyme, the most predominant clinical mutation in Canavan disease, while having a negligible effect on the native enzyme. Based on the initial successes, some structural analogs of these initial hits were selected for further examination. Glutathione, NAAG and patulin were each confirmed to be competitive inhibitors, indicating the binding of these compounds at the dimer interface or near the active site of the E285A enzyme. The experimental results were theoretically examined with the help of the docking analysis method. The structure activity-guided optimization of these compounds can potentially lead to potential pharmacological chaperones that could alleviate the detrimental effect of ASPA mutations in Canavan patients.
被引量：- 发表：1970
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Kinetic characterization of the C-terminal domain of Malonyl-CoA reductase.
Malonyl-CoA reductase utilizes two equivalents of NADPH to catalyze the reduction of malonyl-CoA to 3-hydroxypropionic acid (3HP). This reaction is part of the carbon fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus. The enzyme is composed of two domains. The C-terminal domain catalyzes the reduction of malonyl-CoA to malonic semialdehyde, while the N-terminal domain catalyzes the reduction of the aldehyde to 3HP. The two domains can be produced independently and retain their enzymatic activity. This report focuses on the kinetic characterization of the C-terminal domain. Initial velocity patterns and inhibition studies showed the kinetic mechanism is ordered with NADPH binding first followed by malonyl-CoA. Malonic semialdehyde is released first, while CoA and NADP+ are released randomly. Analogs of malonyl-CoA showed that the thioester carbon is reduced, while the carboxyl group is needed for proper positioning. The enzyme transfers the pro-S hydrogen of NADPH to malonyl-CoA and pH rate profiles revealed that a residue with a pKa value of about 8.8 must be protonated for activity. Kinetic isotope effects indicated that NADPH is not sticky (that is, NADPH dissociates from the enzyme faster than the rate of product formation) and product release is partially rate-limiting. Moreover, the mechanism is stepwise with the pH dependent step occurring before or after hydride transfer. The findings from this study will aid in the development of an eco-friendly biosynthesis of 3HP which is an industrial chemical used in the production of plastics and adhesives.
被引量：- 发表：1970
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Exploring liquid-liquid phase separation in the organisation of Golgi matrix proteins.
The Golgi apparatus is a critical organelle in protein sorting and lipid metabolism. Characterized by its stacked, flattened cisternal structure, the Golgi exhibits distinct polarity with its cis- and trans-faces orchestrating various protein maturation and transport processes. At the heart of its structural integrity and organisation are the Golgi Matrix Proteins (GMPs), predominantly comprising Golgins and GRASPs. These proteins contribute to this organelle's unique stacked and polarized structure and ensure the precise localization of Golgi-resident enzymes, which is crucial for accurate protein processing. Despite over a century of research since its discovery, the Golgi architecture's intricate mechanisms still need to be fully understood. Here, we discuss that GMPs across different Eukaryotic lineages present a significant tendency to form biomolecular condensates. Moreover, we validated experimentally that members of the GRASP family also exhibit a strong tendency. Our findings offer a new perspective on the possible roles of protein disorder and condensation of GMPs in the Golgi organisation.
被引量：1 发表：1970
