FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2125206569> ?p ?o ?g. }

• W2125206569 endingPage "21133" @default.
• W2125206569 startingPage "21126" @default.
• W2125206569 abstract "Pyrrolnitrin (3-chloro-4-(2′-nitro-3′-chlorophenyl)pyrrole) is a broad-spectrum antifungal compound isolated from Pseudomonas pyrrocinia. Four enzymes (PrnA, PrnB, PrnC, and PrnD) are required for pyrrolnitrin biosynthesis from tryptophan. PrnB rearranges the indole ring of 7-Cl-l-tryptophan and eliminates the carboxylate group. PrnB shows robust activity in vivo, but in vitro activity for PrnB under defined conditions remains undetected. The structure of PrnB establishes that the enzyme belongs to the heme b-dependent indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) family. We report the cyanide complex of PrnB and two ternary complexes with both l-tryptophan or 7-Cl-l-tryptophan and cyanide. The latter two complexes are essentially identical and mimic the likely catalytic ternary complex that occurs during turnover. In the cyanide ternary complexes, a loop previously disordered becomes ordered, contributing to the binding of substrates. The conformations of the bound tryptophan substrates are changed from that seen previously in the binary complexes. In l-tryptophan ternary complex, the indole ring now adopts the same orientation as seen in the PrnB binary complexes with other tryptophan substrates. The amide and carboxylate group of the substrate are orientated in a new conformation. Tyr321 and Ser332 play a key role in binding these groups. The structures suggest that catalysis requires an l-configured substrate. Isothermal titration calorimetry data suggest d-tryptophan does not bind after cyanide (or oxygen) coordinates with the distal (or sixth) site of heme. This is the first ternary complex with a tryptophan substrate of a member of the tryptophan dioxygenase superfamily and has mechanistic implications. Pyrrolnitrin (3-chloro-4-(2′-nitro-3′-chlorophenyl)pyrrole) is a broad-spectrum antifungal compound isolated from Pseudomonas pyrrocinia. Four enzymes (PrnA, PrnB, PrnC, and PrnD) are required for pyrrolnitrin biosynthesis from tryptophan. PrnB rearranges the indole ring of 7-Cl-l-tryptophan and eliminates the carboxylate group. PrnB shows robust activity in vivo, but in vitro activity for PrnB under defined conditions remains undetected. The structure of PrnB establishes that the enzyme belongs to the heme b-dependent indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) family. We report the cyanide complex of PrnB and two ternary complexes with both l-tryptophan or 7-Cl-l-tryptophan and cyanide. The latter two complexes are essentially identical and mimic the likely catalytic ternary complex that occurs during turnover. In the cyanide ternary complexes, a loop previously disordered becomes ordered, contributing to the binding of substrates. The conformations of the bound tryptophan substrates are changed from that seen previously in the binary complexes. In l-tryptophan ternary complex, the indole ring now adopts the same orientation as seen in the PrnB binary complexes with other tryptophan substrates. The amide and carboxylate group of the substrate are orientated in a new conformation. Tyr321 and Ser332 play a key role in binding these groups. The structures suggest that catalysis requires an l-configured substrate. Isothermal titration calorimetry data suggest d-tryptophan does not bind after cyanide (or oxygen) coordinates with the distal (or sixth) site of heme. This is the first ternary complex with a tryptophan substrate of a member of the tryptophan dioxygenase superfamily and has mechanistic implications." @default.
• W2125206569 created "2016-06-24" @default.
• W2125206569 creator A5028467044 @default.
• W2125206569 creator A5030620788 @default.
• W2125206569 creator A5078371318 @default.
• W2125206569 date "2010-07-01" @default.
• W2125206569 modified "2023-10-06" @default.
• W2125206569 title "The Ternary Complex of PrnB (the Second Enzyme in the Pyrrolnitrin Biosynthesis Pathway), Tryptophan, and Cyanide Yields New Mechanistic Insights into the Indolamine Dioxygenase Superfamily" @default.
• W2125206569 cites W1597117184 @default.
• W2125206569 cites W1906899252 @default.
• W2125206569 cites W1967372919 @default.
• W2125206569 cites W1999089069 @default.
• W2125206569 cites W1999590520 @default.
• W2125206569 cites W2009930767 @default.
• W2125206569 cites W2018058993 @default.
• W2125206569 cites W2024465426 @default.
• W2125206569 cites W2031515439 @default.
• W2125206569 cites W2041411283 @default.
• W2125206569 cites W2059007464 @default.
• W2125206569 cites W2073298766 @default.
• W2125206569 cites W2074495555 @default.
• W2125206569 cites W2074794066 @default.
• W2125206569 cites W2082227814 @default.
• W2125206569 cites W2083450633 @default.
• W2125206569 cites W2101634195 @default.
• W2125206569 cites W2103968973 @default.
• W2125206569 cites W2108048523 @default.
• W2125206569 cites W2114367386 @default.
• W2125206569 cites W2122273656 @default.
• W2125206569 cites W2122339645 @default.
• W2125206569 cites W2139205312 @default.
• W2125206569 cites W2144081223 @default.
• W2125206569 cites W2148408045 @default.
• W2125206569 cites W2152524078 @default.
• W2125206569 cites W2159673356 @default.
• W2125206569 cites W2163839853 @default.
• W2125206569 cites W2171920440 @default.
• W2125206569 doi "https://doi.org/10.1074/jbc.m110.120485" @default.
• W2125206569 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2898318" @default.
• W2125206569 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20421301" @default.
• W2125206569 hasPublicationYear "2010" @default.
• W2125206569 type Work @default.
• W2125206569 sameAs 2125206569 @default.
• W2125206569 citedByCount "27" @default.
• W2125206569 countsByYear W21252065692012 @default.
• W2125206569 countsByYear W21252065692013 @default.
• W2125206569 countsByYear W21252065692014 @default.
• W2125206569 countsByYear W21252065692015 @default.
• W2125206569 countsByYear W21252065692016 @default.
• W2125206569 countsByYear W21252065692017 @default.
• W2125206569 countsByYear W21252065692018 @default.
• W2125206569 countsByYear W21252065692019 @default.
• W2125206569 countsByYear W21252065692020 @default.
• W2125206569 countsByYear W21252065692021 @default.
• W2125206569 countsByYear W21252065692023 @default.
• W2125206569 crossrefType "journal-article" @default.
• W2125206569 hasAuthorship W2125206569A5028467044 @default.
• W2125206569 hasAuthorship W2125206569A5030620788 @default.
• W2125206569 hasAuthorship W2125206569A5078371318 @default.
• W2125206569 hasBestOaLocation W21252065691 @default.
• W2125206569 hasConcept C156911925 @default.
• W2125206569 hasConcept C178790620 @default.
• W2125206569 hasConcept C181199279 @default.
• W2125206569 hasConcept C185592680 @default.
• W2125206569 hasConcept C192527728 @default.
• W2125206569 hasConcept C2776706248 @default.
• W2125206569 hasConcept C2776834422 @default.
• W2125206569 hasConcept C2778074193 @default.
• W2125206569 hasConcept C2778455166 @default.
• W2125206569 hasConcept C515207424 @default.
• W2125206569 hasConcept C55493867 @default.
• W2125206569 hasConcept C71240020 @default.
• W2125206569 hasConcept C86756495 @default.
• W2125206569 hasConceptScore W2125206569C156911925 @default.
• W2125206569 hasConceptScore W2125206569C178790620 @default.
• W2125206569 hasConceptScore W2125206569C181199279 @default.
• W2125206569 hasConceptScore W2125206569C185592680 @default.
• W2125206569 hasConceptScore W2125206569C192527728 @default.
• W2125206569 hasConceptScore W2125206569C2776706248 @default.
• W2125206569 hasConceptScore W2125206569C2776834422 @default.
• W2125206569 hasConceptScore W2125206569C2778074193 @default.
• W2125206569 hasConceptScore W2125206569C2778455166 @default.
• W2125206569 hasConceptScore W2125206569C515207424 @default.
• W2125206569 hasConceptScore W2125206569C55493867 @default.
• W2125206569 hasConceptScore W2125206569C71240020 @default.
• W2125206569 hasConceptScore W2125206569C86756495 @default.
• W2125206569 hasIssue "27" @default.
• W2125206569 hasLocation W21252065691 @default.
• W2125206569 hasLocation W21252065692 @default.
• W2125206569 hasLocation W21252065693 @default.
• W2125206569 hasLocation W21252065694 @default.
• W2125206569 hasOpenAccess W2125206569 @default.
• W2125206569 hasPrimaryLocation W21252065691 @default.
• W2125206569 hasRelatedWork W1973786713 @default.
• W2125206569 hasRelatedWork W1976259414 @default.
• W2125206569 hasRelatedWork W1995545479 @default.
• W2125206569 hasRelatedWork W2020980248 @default.
• W2125206569 hasRelatedWork W2027501925 @default.

• next