Structure of the O-polysaccharide of Photorhabdus luminescens subsp. laumondii containing d-glycero-d-manno-heptose and 3,6-dideoxy-3-formamido-d-glucose

Kondakova, Anna N.; Kirsheva, Nadezhda A.; Shashkov, Alexander S.; Shaikhutdinova, Rima Z.; Arbatsky, Nikolay P.; Ivanov, Sergey A.; Anisimov, Andrey P.; Knirel, Yuriy A.

doi:10.1016/j.carres.2012.01.021

Cited by 6 publications

(2 citation statements)

References 12 publications

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“…As expected, the largest difference between chemical shifts of Z - and E -isomers (Δδ H 0.40 ppm, Δδ C 5.0 ppm) was observed for the C/H pair at the position of attachment of the formyl group (position 4). A similarly large effect on 13 C NMR signals of an N-formylated sugar was reported previously for 3,6-dideoxy-4-formamido- d -glucose (Qui3NFo), although in other cases the difference between 13 C NMR data of the two stereoisomers can be less pronounced …”

Section: Resultssupporting

confidence: 82%

Structural Insight into a Novel Formyltransferase and Evolution to a Nonribosomal Peptide Synthetase Tailoring Domain

et al. 2018

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Nonribosomal peptide synthetases (NRPSs) increase the chemical diversity of their products by acquiring tailoring domains. Linear gramicidin synthetase starts with a tailoring formylation (F) domain, which likely originated from a sugar formyltransferase (FT) gene. Here, we present studies on an Anoxybacillus kamchatkensis sugar FT representative of the prehorizontal gene transfer FT. Gene cluster analysis reveals that this FT acts on a UDP-sugar in a novel pathway for synthesis of a 7-formamido derivative of CMP-pseudaminic acid. We recapitulate the pathway up to and including the formylation step in vitro, experimentally demonstrating the role of the FT. We also present X-ray crystal structures of the FT alone and with ligands, which unveil contrasts with other structurally characterized sugar FTs and show close structural similarity with the F domain. The structures reveal insights into the adaptations that were needed to co-opt and evolve a sugar FT into a functional and useful NRPS domain.

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Section: Resultssupporting

confidence: 82%

Structural Insight into a Novel Formyltransferase and Evolution to a Nonribosomal Peptide Synthetase Tailoring Domain

et al. 2018

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“…At present, a major limitation to substrate specificity characterization in these putative homologues is that the O-Ag compositions and/or structures from the respective bacterial strains have yet to be elucidated. Despite extensive searching, we were only able to find an O-Ag chemical structure37 for one of the strains ( Photorhabdus luminescens subsp. laumondii TT01) identified in the list of non-redundant Wzy Pa sequence hits; unfortunately, no chemical or topological similarities could be found between this particular O-Ag structure and that of the B-band O-Ag of P. aeruginosa PAO1.…”

Section: Discussionmentioning

confidence: 99%

Conserved-residue mutations in Wzy affect O-antigen polymerization and Wzz-mediated chain-length regulation in Pseudomonas aeruginosa PAO1

Islam

Huszczynski

Nugent

et al. 2013

Sci Rep

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O antigen (O-Ag) in many bacteria is synthesized via the Wzx/Wzy-dependent pathway in which Wzy polymerizes lipid-linked O-Ag subunits to modal lengths regulated by Wzz. Characterization of 83 site-directed mutants of Wzy from Pseudomonas aeruginosa PAO1 (WzyPa) in topologically-mapped periplasmic (PL) and cytoplasmic loops (CL) verified the functional importance of PL3 and PL5, with the former shown to require overall cationic properties. Essential Arg residues in the RX10G motifs of PL3 and PL5 were found to be conserved in putative homologues of WzyPa, as was the overall sequence homology between these two periplasmic loops in each protein. Amino acid substitutions in CL6 were found to alter Wzz-mediated O-antigen modality, with evidence suggesting that these changes may perturb the C-terminal WzyPa tertiary structure. Together, these data suggest that the catch-and-release mechanism of O-Ag polymerization is widespread among bacteria and that regulation of polymer length is affected by interaction of Wzz with Wzy.

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Structure of the O-polysaccharide of Photorhabdus temperata subsp. temperata XlNachT containing a novel branched monosaccharide, 3,6-dideoxy-4-C-[(S)-1,2-dihydroxyethyl]-d-xylo-hexose

Arbatsky

Shashkov

Kirsheva

et al. 2015

Carbohydrate Research

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Structure of the O-polysaccharide of Photorhabdus luminescens subsp. laumondii containing d-glycero-d-manno-heptose and 3,6-dideoxy-3-formamido-d-glucose

Cited by 6 publications

References 12 publications

Structural Insight into a Novel Formyltransferase and Evolution to a Nonribosomal Peptide Synthetase Tailoring Domain

Structural Insight into a Novel Formyltransferase and Evolution to a Nonribosomal Peptide Synthetase Tailoring Domain

Conserved-residue mutations in Wzy affect O-antigen polymerization and Wzz-mediated chain-length regulation in Pseudomonas aeruginosa PAO1

Structure of the O-polysaccharide of Photorhabdus temperata subsp. temperata XlNachT containing a novel branched monosaccharide, 3,6-dideoxy-4-C-[(S)-1,2-dihydroxyethyl]-d-xylo-hexose

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