FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2034453583> ?p ?o ?g. }

• W2034453583 endingPage "1116" @default.
• W2034453583 startingPage "1107" @default.
• W2034453583 abstract "Background: Sequence alignment suggests that xylanases evolved from two ancestral proteins and therefore can be grouped into two families, designated F and G. Family F enzymes show no sequence similarity with any known structure and their architecture is unknown. Studies of an inactive enzyme–substrate complex will help to elucidate the structural basis of binding and catalysis in the family F xylanases.Results We have therefore determined the crystal structure of the catalytic domain of a family F enzyme, Pseudomonas fluorescens subsp. cellulosa xylanase A, at 2.5 Å resolution and a crystallographic R-factor of 0.20. The structure was solved using an engineered cata lytic core in which the nucleophilic glutamate was replaced by a cysteine. As expected, this yielded both high-quality mercurial derivatives and an inactive enzym e which enabled the preparation of the inactive enzyme–substrate complex in the crystal. We show that family F xylanases are eight-fold α/β-barrels (TIM barrels) with two active-site glutamates, one of which is the nucleophile and the other the acid-base. Xylopentaose binds to five subsites A–E with the cleaved bond between subsites D and E. Ca2+ binding, remote from the active-site glutamates, stabilizes the structure and may be involved in the binding of extended substrates.Conclusion The architecture of P. fluorescens subsp. cellulosa has been determined crystallographically to be a commonly occurring enzyme fold, the eight-fold α/β-barrel. Xylopentaose binds across the carboxy-terminal end of the α/β-barrel in an active-site cleft which contains the two catalytic glutamates." @default.
• W2034453583 created "2016-06-24" @default.
• W2034453583 creator A5004810388 @default.
• W2034453583 creator A5019613781 @default.
• W2034453583 creator A5027476978 @default.
• W2034453583 creator A5029283940 @default.
• W2034453583 creator A5040646162 @default.
• W2034453583 creator A5042010650 @default.
• W2034453583 creator A5045334542 @default.
• W2034453583 creator A5059560909 @default.
• W2034453583 creator A5060174826 @default.
• W2034453583 creator A5077829519 @default.
• W2034453583 date "1994-11-01" @default.
• W2034453583 modified "2023-09-27" @default.
• W2034453583 title "Structure of the catalytic core of the family F xylanase from Pseudomonas fluorescens and identification of the xylopentaose-binding sites" @default.
• W2034453583 cites W1525347874 @default.
• W2034453583 cites W1525745093 @default.
• W2034453583 cites W154700294 @default.
• W2034453583 cites W1574246355 @default.
• W2034453583 cites W1899953143 @default.
• W2034453583 cites W1975914851 @default.
• W2034453583 cites W1978928219 @default.
• W2034453583 cites W1982843556 @default.
• W2034453583 cites W1987435352 @default.
• W2034453583 cites W1993404146 @default.
• W2034453583 cites W2002572115 @default.
• W2034453583 cites W2013083986 @default.
• W2034453583 cites W2015478270 @default.
• W2034453583 cites W2024594001 @default.
• W2034453583 cites W2028231353 @default.
• W2034453583 cites W2034865738 @default.
• W2034453583 cites W2036931150 @default.
• W2034453583 cites W2037410079 @default.
• W2034453583 cites W2066459154 @default.
• W2034453583 cites W2071486470 @default.
• W2034453583 cites W2077365386 @default.
• W2034453583 cites W2080476827 @default.
• W2034453583 cites W2088144279 @default.
• W2034453583 cites W2088913176 @default.
• W2034453583 cites W2095237995 @default.
• W2034453583 cites W2099942609 @default.
• W2034453583 cites W2113964973 @default.
• W2034453583 cites W2151900576 @default.
• W2034453583 cites W2157165549 @default.
• W2034453583 cites W2950469006 @default.
• W2034453583 cites W4229959333 @default.
• W2034453583 doi "https://doi.org/10.1016/s0969-2126(94)00112-x" @default.
• W2034453583 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7881909" @default.
• W2034453583 hasPublicationYear "1994" @default.
• W2034453583 type Work @default.
• W2034453583 sameAs 2034453583 @default.
• W2034453583 citedByCount "127" @default.
• W2034453583 countsByYear W20344535832012 @default.
• W2034453583 countsByYear W20344535832013 @default.
• W2034453583 countsByYear W20344535832014 @default.
• W2034453583 countsByYear W20344535832015 @default.
• W2034453583 countsByYear W20344535832016 @default.
• W2034453583 countsByYear W20344535832017 @default.
• W2034453583 countsByYear W20344535832018 @default.
• W2034453583 countsByYear W20344535832019 @default.
• W2034453583 countsByYear W20344535832021 @default.
• W2034453583 countsByYear W20344535832022 @default.
• W2034453583 countsByYear W20344535832023 @default.
• W2034453583 crossrefType "journal-article" @default.
• W2034453583 hasAuthorship W2034453583A5004810388 @default.
• W2034453583 hasAuthorship W2034453583A5019613781 @default.
• W2034453583 hasAuthorship W2034453583A5027476978 @default.
• W2034453583 hasAuthorship W2034453583A5029283940 @default.
• W2034453583 hasAuthorship W2034453583A5040646162 @default.
• W2034453583 hasAuthorship W2034453583A5042010650 @default.
• W2034453583 hasAuthorship W2034453583A5045334542 @default.
• W2034453583 hasAuthorship W2034453583A5059560909 @default.
• W2034453583 hasAuthorship W2034453583A5060174826 @default.
• W2034453583 hasAuthorship W2034453583A5077829519 @default.
• W2034453583 hasBestOaLocation W20344535831 @default.
• W2034453583 hasConcept C107824862 @default.
• W2034453583 hasConcept C139489369 @default.
• W2034453583 hasConcept C181199279 @default.
• W2034453583 hasConcept C185592680 @default.
• W2034453583 hasConcept C2775859485 @default.
• W2034453583 hasConcept C2776835041 @default.
• W2034453583 hasConcept C2780120296 @default.
• W2034453583 hasConcept C41183919 @default.
• W2034453583 hasConcept C47701112 @default.
• W2034453583 hasConcept C523546767 @default.
• W2034453583 hasConcept C54355233 @default.
• W2034453583 hasConcept C55493867 @default.
• W2034453583 hasConcept C71240020 @default.
• W2034453583 hasConcept C8010536 @default.
• W2034453583 hasConcept C86803240 @default.
• W2034453583 hasConceptScore W2034453583C107824862 @default.
• W2034453583 hasConceptScore W2034453583C139489369 @default.
• W2034453583 hasConceptScore W2034453583C181199279 @default.
• W2034453583 hasConceptScore W2034453583C185592680 @default.
• W2034453583 hasConceptScore W2034453583C2775859485 @default.
• W2034453583 hasConceptScore W2034453583C2776835041 @default.
• W2034453583 hasConceptScore W2034453583C2780120296 @default.
• W2034453583 hasConceptScore W2034453583C41183919 @default.

• next