Articles with "ser thr" as a keyword



Escherichia coli YegI is a novel Ser/Thr kinase lacking conserved motifs that localizes to the inner membrane

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Published in 2020 at "FEBS Letters"

DOI: 10.1002/1873-3468.13920

Abstract: In bacteria, signaling phosphorylation is thought to occur primarily on His and Asp residues. However, phosphoproteomic surveys in phylogenetically diverse bacteria over the past decade have identified numerous proteins that are phosphorylated on Ser and/or… read more here.

Keywords: escherichia coli; thr; thr kinase; novel ser ... See more keywords

Self‐contacting Cys, Ser, and Thr residues in high‐resolution protein crystal structures: Tertiary constraints or hydrogen bonds?

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Published in 2024 at "Protein Science"

DOI: 10.1002/pro.5218

Abstract: Functional groups in the side‐chains of at least 10 amino acids are mainly involved in tertiary interactions. However, structural and functional significance of intra‐residue interactions has not been fully recognized. In this study, we have… read more here.

Keywords: contacting cys; hydrogen bonds; thr residues; ser thr ... See more keywords
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When are two hydrogen bonds better than one? Accurate first-principles models explain the balance of hydrogen bond donors and acceptors found in proteins

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Published in 2021 at "Chemical Science"

DOI: 10.1039/d0sc05084a

Abstract: Hydrogen bonds (HBs) play an essential role in the structure and catalytic action of enzymes, but a complete understanding of HBs in proteins challenges the resolution of modern structural (i.e., X-ray diffraction) techniques and mandates… read more here.

Keywords: hba hbd; hydrogen; hydrogen bonds; two hydrogen ... See more keywords

Prior disulfide bond-mediated Ser/Thr ligation.

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Published in 2024 at "Chemical science"

DOI: 10.1039/d4sc04825c

Abstract: In this work, we developed a novel strategy, prior disulfide bond-mediated Ser/Thr ligation (PD-STL), for the chemical synthesis of peptides and proteins. This approach combines disulfide bond-forming chemistry with Ser/Thr ligation (STL), converting intermolecular STL… read more here.

Keywords: ligation; disulfide bond; thr ligation; prior disulfide ... See more keywords

Structural model of the full-length Ser/Thr protein kinase StkP from S. pneumoniae and its recognition of peptidoglycan fragments

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Published in 2018 at "Journal of Biomolecular Structure and Dynamics"

DOI: 10.1080/07391102.2017.1395767

Abstract: The unique eukaryotic-like Ser/Thr protein kinases of Streptococcus pneumoniae, StkP, plays a primary role in the cell division process. It is composed of an intracellular kinase domain, a transmembrane helix and four extracellular PASTA subunits.… read more here.

Keywords: full length; structural model; model; thr protein ... See more keywords
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Wedelolactone facilitates Ser/Thr phosphorylation of NLRP3 dependent on PKA signalling to block inflammasome activation and pyroptosis

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Published in 2020 at "Cell Proliferation"

DOI: 10.1111/cpr.12868

Abstract: Wedelolactone exhibits regulatory effects on some inflammatory diseases. However, the anti‐inflammatory mechanism of wedelolactone has not been entirely unravelled. Therefore, the present study focuses on investigating the mechanism of wedelolactone on NLRP3 inflammasome in macrophages… read more here.

Keywords: thr phosphorylation; facilitates ser; wedelolactone; wedelolactone facilitates ... See more keywords

E. coli Toxin YjjJ (HipH) Is a Ser/Thr Protein Kinase That Impacts Cell Division, Carbon Metabolism, and Ribosome Assembly

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Published in 2022 at "mSystems"

DOI: 10.1128/msystems.01043-22

Abstract: Adaptation to growth condition is the key for bacterial survival, and protein phosphorylation is one of the strategies adopted to transduce extracellular signal in physiological response. In a previous work, we identified YjjJ, a putative… read more here.

Keywords: ser thr; yjjj; kinase; protein ... See more keywords

Intracellular Ser/Thr/Tyr phosphoproteome of the oral commensal Streptococcus gordonii DL1

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Published in 2020 at "BMC Microbiology"

DOI: 10.1186/s12866-020-01944-y

Abstract: Background To respond and adapt to environmental challenges, prokaryotes regulate cellular processes rapidly and reversibly through protein phosphorylation and dephosphorylation. This study investigates the intracellular proteome and Ser/Thr/Tyr phosphoproteome of the oral commensal Streptococcus gordonii.… read more here.

Keywords: thr tyr; gordonii dl1; streptococcus; ser thr ... See more keywords

The Phosphorylation of CCR6 on Distinct Ser/Thr Residues in the Carboxyl Terminus Differentially Regulates Biological Function

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Published in 2018 at "Frontiers in Immunology"

DOI: 10.3389/fimmu.2018.00415

Abstract: CCR6 is a G protein-coupled receptor (GPCR) that recognizes a single chemokine ligand, CCL20 and is primarily expressed by leukocytes. Upon ligand binding, CCR6 activates Gαi heterotrimeric G proteins to induce various potential cellular outcomes… read more here.

Keywords: thr residues; ccr6; phosphorylation; ser thr ... See more keywords

Mycobacterium tuberculosis Thymidylyltransferase RmlA Is Negatively Regulated by Ser/Thr Protein Kinase PknB

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Published in 2021 at "Frontiers in Microbiology"

DOI: 10.3389/fmicb.2021.643951

Abstract: Ser/Thr phosphorylation by serine/threonine protein kinases (STPKs) plays significant roles in molecular regulation, which allows Mycobacteria to adapt their cell wall structure in response to the environment changes. Identifying direct targets of STPKs and determining… read more here.

Keywords: ser thr; thr; cell wall; rmla ... See more keywords

Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases—United in Diversity

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Published in 2022 at "Biomolecules"

DOI: 10.3390/biom12101346

Abstract: To clarify the obscure hydrolysis mechanism of ubiquitous P-loop-fold nucleoside triphosphatases (Walker NTPases), we analysed the structures of 3136 catalytic sites with bound Mg-NTP complexes or their analogues. Our results are presented in two articles;… read more here.

Keywords: loop fold; fold nucleoside; loop; ser thr ... See more keywords