![pbp3 ftsi uniprot pbp3 ftsi uniprot](https://www.researchgate.net/publication/337406139/figure/fig1/AS:827479061196800@1574297790148/PBP3-crystal-structure-analysis-a-Crystal-structure-alignment-of-621-PBP3-of_Q320.jpg)
These elements correspond to the DSSP secondary structure code 'T'.More. This subsection of the 'Structure' section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence.
![pbp3 ftsi uniprot pbp3 ftsi uniprot](https://www.researchgate.net/profile/Antonio-Frandi/publication/261443806/figure/fig4/AS:289141012090932@1445947997512/RodZ-accumulates-at-the-division-septum-earlier-during-division-than-MreB-a-Dividing.png)
This subsection of the 'Structure' section is used to indicate the positions of experimentally determined helical regions within the protein i
#Pbp3 ftsi uniprot manual#
Information inferred from a combination of experimental and computational evidence, without manual validation.Īutomatic assertion inferred from combination of experimental and computational evidence i This subsection of the 'Structure' section is used to indicate the positions of experimentally determined beta strands within the protein strand i Legend: Helix Turn Beta strand PDB Structure known for this area Show more details Hide details Feature key It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed lineage iĬellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas aeruginosa group › Pseudomonas aeruginosa Genetic analysis of the cell division protein FtsI (PBP3): amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN. This subsection of the Names and taxonomy section contains the taxonomic hierarchical classification lineage of the source organism. This is known as the 'taxonomic identifier' or 'taxid'.More.Taxonomic identifier i This subsection of the Names and taxonomy section shows the unique identifier assigned by the NCBI to the source organism of the protein. This subsection of the Names and taxonomy section provides information on the name(s) of the organism that is the source of the protein i Manual assertion inferred from database entries i
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Manually validated information which has been imported from another database. Inferred from biological aspect of ancestor i More information in the GO evidence code guide
![pbp3 ftsi uniprot pbp3 ftsi uniprot](https://europepmc.org/articles/PMC3025346/bin/fx1.jpg)
Inferred from Biological aspect of AncestorĪ type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene. The Gene Ontology (GO) project provides a set of hierarchical controlled vocabulary split into 3 categories:More.GO - Molecular function i This subsection of the Function section is used for enzymes and indicates the residues directly involved in site iĪcyl-ester intermediate UniRule annotation View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis. School of Life Sciences, University of Warwick, Coventry CV4 7AL, U.K.This subsection of the 'Function' section describes the metabolic pathway(s) associated with a i: peptidoglycan biosynthesisThis protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis. Overall, the results further evidence the potential for the development of new classes of boron-based antibiotics, which are not compromised by β-lactamase-driven resistance. Modifications of the benzoxaborole scaffold resulted in a moderately potent inhibition of PaPBP3, though no antibacterial activity was observed. Multiple crystal structures reveal that boronic acids react with PBPs to give tricovalently linked complexes bonded to Ser294, Ser349, and Lys484 of PaPBP3 benzoxaboroles react with PaPBP3 via reaction with two nucleophilic serines (Ser294 and Ser349) to give dicovalently linked complexes and vaborbactam reacts to give a monocovalently linked complex. We used high-throughput X-ray crystallography to explore reactions of a boron-containing fragment set with the Pseudomonas aeruginosa PBP3 (PaPBP3). Boron-containing inhibitors are potent serine-β-lactamase inhibitors, but the interactions of boron-based compounds with the penicillin-binding protein (PBP) β-lactam targets have not been extensively studied. The effectiveness of β-lactam antibiotics is increasingly compromised by β-lactamases.