About: Crystal Structure of Haloalkane Dehalogenase LinB from Sphingomonas paucimobilis UT26 at 0.95 A Resolution: Dynamics of Catalytic Residues     Goto   Sponge   NotDistinct   Permalink

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Description
  • Zkoumali jsme strukturu LinB 33 kDa haloalkándehalogenázy z bakterie Sphingomonas paucimobilis UT26,při rozlišení 0.95 A. Námi ziskaná data přímo poukázaly anizotropní pohyb katalytických zbytků. (cs)
  • We present the structure of LinB, a 33 kDa haloalkane dehalogenase from Sphingomonas paucimobilis UT26, at 0.95 A resolution. The data have allowed us to directly observe the anisotropic motions of the catalytic residues. In particular, the side-chain of the catalytic nucleophile, Asp108, displays a high degree of disorder. It has been modeled in two conformations, one similar to that observed previously (conformation A) and one strained (conformation B) that approached the catalytic base (His272). The strain in the conformation B was mainly in the Ca-Cb-Cg angle (126) that deviated by 13.4 from the "ideal" bond angle of 112.6. Based on these observations, we propose a role for the charge state of the catalytic histidine in determining the geometry of the catalytic residues. We hypothesized that double-protonation of the catalytic base (His272) reduces the distance between the side-chain of this residue and that of the Asp108. The results of molecular dynamics simulations were consistent wit
  • We present the structure of LinB, a 33 kDa haloalkane dehalogenase from Sphingomonas paucimobilis UT26, at 0.95 A resolution. The data have allowed us to directly observe the anisotropic motions of the catalytic residues. In particular, the side-chain of the catalytic nucleophile, Asp108, displays a high degree of disorder. It has been modeled in two conformations, one similar to that observed previously (conformation A) and one strained (conformation B) that approached the catalytic base (His272). The strain in the conformation B was mainly in the Ca-Cb-Cg angle (126) that deviated by 13.4 from the "ideal" bond angle of 112.6. Based on these observations, we propose a role for the charge state of the catalytic histidine in determining the geometry of the catalytic residues. We hypothesized that double-protonation of the catalytic base (His272) reduces the distance between the side-chain of this residue and that of the Asp108. The results of molecular dynamics simulations were consistent wit (en)
Title
  • Crystal Structure of Haloalkane Dehalogenase LinB from Sphingomonas paucimobilis UT26 at 0.95 A Resolution: Dynamics of Catalytic Residues
  • Crystal Structure of Haloalkane Dehalogenase LinB from Sphingomonas paucimobilis UT26 at 0.95 A Resolution: Dynamics of Catalytic Residues (en)
  • Krystalová struktura haloalkán dehalogenázy LinB z Sphingomonas paucimobilis UT26 při rozlišení 0,94 A: funkční a katalytické zbytky. (cs)
skos:prefLabel
  • Crystal Structure of Haloalkane Dehalogenase LinB from Sphingomonas paucimobilis UT26 at 0.95 A Resolution: Dynamics of Catalytic Residues
  • Crystal Structure of Haloalkane Dehalogenase LinB from Sphingomonas paucimobilis UT26 at 0.95 A Resolution: Dynamics of Catalytic Residues (en)
  • Krystalová struktura haloalkán dehalogenázy LinB z Sphingomonas paucimobilis UT26 při rozlišení 0,94 A: funkční a katalytické zbytky. (cs)
skos:notation
  • RIV/00216224:14310/04:00010578!RIV08-MSM-14310___
http://linked.open.../vavai/riv/strany
  • 870-878
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(MSM 143100005)
http://linked.open...iv/cisloPeriodika
  • 43
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
  • 559041
http://linked.open...ai/riv/idVysledku
  • RIV/00216224:14310/04:00010578
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • Crystal structure; Haloalkane Dehalogenase; LinB (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [84CFE10D3C26]
http://linked.open...i/riv/nazevZdroje
  • Biochemistry
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 43
http://linked.open...iv/tvurceVysledku
  • Damborský, Jiří
  • Klvaňa, Martin
  • Nagata, Yuji
  • Otyepka, Michal
  • Oakley, Aaron
  • Wilce, Matthew
http://linked.open...n/vavai/riv/zamer
issn
  • 0006-2960
number of pages
http://localhost/t...ganizacniJednotka
  • 14310
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