About: Functionally relevant motions of haloalkane dehalogenases occur in the specificity-modulating cap domains     Goto   Sponge   NotDistinct   Permalink

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Description
  • One nanosecond molecular dynamics trajectories of three haloalkane dehalogenases (DhlA, LinB and DhaA) are compared. The main domain was rigid in all three dehalogenases, while the substrate specificity-modulating cap domains showed considerably higher mobility. The functionally relevant motions were spread over entire cap domain in DhlA, while were more localized in LinB and DhaA. The highest amplitude of essential motions of DhlA was noted in the alpha4-helix-loop-alpha4-helix region, formerly proposed to participate in the large conformation change needed for product release. The highest amplitude of essential motions of LinB and DhaA was observed in the random coil prior to helix 4 linking two domains of these proteins. This flexibility is the consequence of modular composition of haloalkane dehalogenases. Two members of the catalytic triad, i.e. the nucleophile and the base, showed very high level of rigidity in all three dehalogenases. This rigidity is essential for their function. One of the ha
  • One nanosecond molecular dynamics trajectories of three haloalkane dehalogenases (DhlA, LinB and DhaA) are compared. The main domain was rigid in all three dehalogenases, while the substrate specificity-modulating cap domains showed considerably higher mobility. The functionally relevant motions were spread over entire cap domain in DhlA, while were more localized in LinB and DhaA. The highest amplitude of essential motions of DhlA was noted in the alpha4-helix-loop-alpha4-helix region, formerly proposed to participate in the large conformation change needed for product release. The highest amplitude of essential motions of LinB and DhaA was observed in the random coil prior to helix 4 linking two domains of these proteins. This flexibility is the consequence of modular composition of haloalkane dehalogenases. Two members of the catalytic triad, i.e. the nucleophile and the base, showed very high level of rigidity in all three dehalogenases. This rigidity is essential for their function. One of the ha (en)
  • One nanosecond molecular dynamics trajectories of three haloalkane dehalogenases (DhlA, LinB and DhaA) are compared. The main domain was rigid in all three dehalogenases, while the substrate specificity-modulating cap domains showed considerably higher mobility. The functionally relevant motions were spread over entire cap domain in DhlA, while were more localized in LinB and DhaA. The highest amplitude of essential motions of DhlA was noted in the alpha4-helix-loop-alpha4-helix region, formerly proposed to participate in the large conformation change needed for product release. The highest amplitude of essential motions of LinB and DhaA was observed in the random coil prior to helix 4 linking two domains of these proteins. This flexibility is the consequence of modular composition of haloalkane dehalogenases. Two members of the catalytic triad, i.e. the nucleophile and the base, showed very high level of rigidity in all three dehalogenases. This rigidity is essential for their function. One of the ha (cs)
Title
  • Functionally relevant motions of haloalkane dehalogenases occur in the specificity-modulating cap domains
  • Functionally relevant motions of haloalkane dehalogenases occur in the specificity-modulating cap domains (en)
  • Functionally relevant motions of haloalkane dehalogenases occur in the specificity-modulating cap domains (cs)
skos:prefLabel
  • Functionally relevant motions of haloalkane dehalogenases occur in the specificity-modulating cap domains
  • Functionally relevant motions of haloalkane dehalogenases occur in the specificity-modulating cap domains (en)
  • Functionally relevant motions of haloalkane dehalogenases occur in the specificity-modulating cap domains (cs)
skos:notation
  • RIV/00216224:14310/02:00006263!RIV08-MSM-14310___
http://linked.open.../vavai/riv/strany
  • 1206
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(LN00A016)
http://linked.open...iv/cisloPeriodika
  • 5
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 646659
http://linked.open...ai/riv/idVysledku
  • RIV/00216224:14310/02:00006263
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • MOLECULAR DYNAMICS; SIMULATION; MOTION; DEHALOGENASE; CATALYSIS (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [B659DCB3030F]
http://linked.open...i/riv/nazevZdroje
  • Protein Science
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 11
http://linked.open...iv/tvurceVysledku
  • Damborský, Jiří
  • Otyepka, Michal
issn
  • 0961-8368
number of pages
http://localhost/t...ganizacniJednotka
  • 14310
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