schliessen

Filtern

 

Bibliotheken

Crystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: Insight into tRNA recognition and reaction mechanism

Hypermodifications near the anticodon of tRNA are fundamental for the efficiency and fidelity of protein synthesis. Dimethylallyltransferase (DMATase) catalyzes transfer of a dimethylallyl moiety from dimethylallyl pyrophosphate to N6 of A37 in certain tRNAs. Here we present the crystal structures o... Full description

Journal Title: Proceedings of the National Academy of Sciences 21 October 2008, Vol.105(42), p.16142
Main Author: Chun Zhou
Other Authors: Raven H. Huang
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0027-8424 ; E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.0805680105
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: pnas_s105_42_16142
title: Crystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: Insight into tRNA recognition and reaction mechanism
format: Article
creator:
  • Chun Zhou
  • Raven H. Huang
subjects:
  • Sciences (General)
ispartof: Proceedings of the National Academy of Sciences, 21 October 2008, Vol.105(42), p.16142
description: Hypermodifications near the anticodon of tRNA are fundamental for the efficiency and fidelity of protein synthesis. Dimethylallyltransferase (DMATase) catalyzes transfer of a dimethylallyl moiety from dimethylallyl pyrophosphate to N6 of A37 in certain tRNAs. Here we present the crystal structures of Saccharomyces cerevisiae DMATase–tRNA Cys complex in four distinct forms, which provide snapshots of the RNA modification reaction catalyzed by DMATase. The structures reveal that the enzyme recognizes the tRNA substrate through indirect sequence readout. The targeted nucleotide A37 flips out from the anticodon loop of tRNA and flips into a channel in DMATase, where it meets its reaction partner di methylallyl pyrophosphate, which enters the channel from the opposite end. Structural changes accompanying the transfer reaction taking place in the crystal result in disengagement of DMATase–tRNA interaction near the reaction center. In addition, structural comparison of DMATase in the complex with unliganded bacterial DMATase provides a molecular basis of ordered substrate binding by DMATase. RNA modification substrate specificity x-ray crystallography
language: eng
source:
identifier: ISSN: 0027-8424 ; E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.0805680105
fulltext: fulltext_linktorsrc
issn:
  • 0027-8424
  • 00278424
  • 1091-6490
  • 10916490
url: Link


@attributes
ID942497002
RANK0.07
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
LOCALfalse
PrimoNMBib
record
control
sourcerecordid105_42_16142
sourceidpnas_s
recordidTN_pnas_s105_42_16142
sourcesystemPC
dbid
0PNE
1RNA
pqid20234234
galeid188997887
display
typearticle
titleCrystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: Insight into tRNA recognition and reaction mechanism
creatorChun Zhou ; Raven H. Huang
ispartofProceedings of the National Academy of Sciences, 21 October 2008, Vol.105(42), p.16142
identifier
subjectSciences (General)
descriptionHypermodifications near the anticodon of tRNA are fundamental for the efficiency and fidelity of protein synthesis. Dimethylallyltransferase (DMATase) catalyzes transfer of a dimethylallyl moiety from dimethylallyl pyrophosphate to N6 of A37 in certain tRNAs. Here we present the crystal structures of Saccharomyces cerevisiae DMATase–tRNA Cys complex in four distinct forms, which provide snapshots of the RNA modification reaction catalyzed by DMATase. The structures reveal that the enzyme recognizes the tRNA substrate through indirect sequence readout. The targeted nucleotide A37 flips out from the anticodon loop of tRNA and flips into a channel in DMATase, where it meets its reaction partner di methylallyl pyrophosphate, which enters the channel from the opposite end. Structural changes accompanying the transfer reaction taking place in the crystal result in disengagement of DMATase–tRNA interaction near the reaction center. In addition, structural comparison of DMATase in the complex with unliganded bacterial DMATase provides a molecular basis of ordered substrate binding by DMATase. RNA modification substrate specificity x-ray crystallography
languageeng
source
version11
lds50peer_reviewed
links
openurl$$Topenurl_article
openurlfulltext$$Topenurlfull_article
linktorsrc$$Uhttp://www.pnas.org/content/105/42/16142.abstract$$EView_full_text_in_National_Academy_of_Sciences_(Access_to_full_text_may_be_restricted)
search
creatorcontrib
0Chun Zhou
1Raven H. Huang
titleCrystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: Insight into tRNA recognition and reaction mechanism
description

Hypermodifications near the anticodon of tRNA are fundamental for the efficiency and fidelity of protein synthesis. Dimethylallyltransferase (DMATase) catalyzes transfer of a dimethylallyl moiety from dimethylallyl pyrophosphate to N6 of A37 in certain tRNAs. Here we present the crystal structures of Saccharomyces cerevisiae DMATase–tRNA Cys complex in four distinct forms, which provide snapshots of the RNA modification reaction catalyzed by DMATase. The structures reveal that the enzyme recognizes the tRNA substrate through indirect sequence readout. The targeted nucleotide A37 flips out from the anticodon loop of tRNA and flips into a channel in DMATase, where it meets its reaction partner di methylallyl pyrophosphate, which enters the channel from the opposite end. Structural changes accompanying the transfer reaction taking place in the crystal result in disengagement of DMATase–tRNA interaction near the reaction center. In addition, structural comparison of DMATase in the complex with unliganded bacterial DMATase provides a molecular basis of ordered substrate binding by DMATase. RNA modification substrate specificity x-ray crystallography

subjectSciences (General)
general
0English
1National Acad Sciences
210.1073/pnas.0805680105
3PNAS (National Academy of Sciences)
4National Academy of Sciences (U.S.)
sourceidpnas_s
recordidpnas_s105_42_16142
issn
00027-8424
100278424
21091-6490
310916490
rsrctypearticle
creationdate2008
addtitleProceedings of the National Academy of Sciences
searchscope
0pnas_full
1pnas4
2pnas5
scope
0pnas_full
1pnas4
2pnas5
lsr45$$EView_full_text_in_National_Academy_of_Sciences_(Access_to_full_text_may_be_restricted)
tmp01
0PNAS (National Academy of Sciences)
1National Academy of Sciences (U.S.)
tmp02
0PNE
1RNA
startdate20081021
enddate20081021
lsr40Proceedings of the National Academy of Sciences, 21 October 2008, Vol.105 (42), p.16142
doi10.1073/pnas.0805680105
citationpf 16142 vol 105 issue 42
lsr30VSR-Enriched:[pqid, galeid, pages]
sort
titleCrystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: Insight into tRNA recognition and reaction mechanism
authorChun Zhou ; Raven H. Huang
creationdate20081021
lso0120081021
facets
frbrgroupid8040329257521626660
frbrtype5
newrecords20190724
languageeng
topicSciences (General)
collection
0PNAS (National Academy of Sciences)
1National Academy of Sciences (U.S.)
prefilterarticles
rsrctypearticles
creatorcontrib
0Chun Zhou
1Raven H. Huang
jtitleProceedings of the National Academy of Sciences
creationdate2008
toplevelpeer_reviewed
delivery
delcategoryRemote Search Resource
fulltextfulltext_linktorsrc
addata
au
0Chun Zhou
1Raven H. Huang
atitleCrystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: Insight into tRNA recognition and reaction mechanism
jtitleProceedings of the National Academy of Sciences
risdate20081021
volume105
issue42
spage16142
issn0027-8424
eissn1091-6490
formatjournal
genrearticle
ristypeJOUR
abstract

Hypermodifications near the anticodon of tRNA are fundamental for the efficiency and fidelity of protein synthesis. Dimethylallyltransferase (DMATase) catalyzes transfer of a dimethylallyl moiety from dimethylallyl pyrophosphate to N6 of A37 in certain tRNAs. Here we present the crystal structures of Saccharomyces cerevisiae DMATase–tRNA Cys complex in four distinct forms, which provide snapshots of the RNA modification reaction catalyzed by DMATase. The structures reveal that the enzyme recognizes the tRNA substrate through indirect sequence readout. The targeted nucleotide A37 flips out from the anticodon loop of tRNA and flips into a channel in DMATase, where it meets its reaction partner di methylallyl pyrophosphate, which enters the channel from the opposite end. Structural changes accompanying the transfer reaction taking place in the crystal result in disengagement of DMATase–tRNA interaction near the reaction center. In addition, structural comparison of DMATase in the complex with unliganded bacterial DMATase provides a molecular basis of ordered substrate binding by DMATase. RNA modification substrate specificity x-ray crystallography

pubNational Acad Sciences
doi10.1073/pnas.0805680105
urlhttp://www.pnas.org/content/105/42/16142.abstract
lad01Proceedings of the National Academy of Sciences
pages16142-16147
date2008-10-21