schliessen

Filtern

 

Bibliotheken

Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition

Lactose permease of Escherichia coli (LacY) with a single-Cys residue in place of A122 (helix IV) transports galactopyranosides and is specifically inactivated by methanethiosulfonyl-galactopyranosides (MTS-gal), which behave as unique suicide substrates. In order to study the mechanism of inactivat... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America 2011, Vol.108(23), pp.9361-9366
Main Author: Chaptal , Vincent
Other Authors: Kwon , Seunghyug , Sawaya , Michael R. , Guan , Lan , Kaback , H. Ronald , Abramson , Jeff
Format: Electronic Article Electronic Article
Language: English
Subjects:
Publisher: National Academy of Sciences
Created: 2011
ID: ISSN: 0027-8424
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: faoagrisUS201600192405
title: Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition
format: Article
creator:
  • Chaptal , Vincent
  • Kwon , Seunghyug
  • Sawaya , Michael R.
  • Guan , Lan
  • Kaback , H. Ronald
  • Abramson , Jeff
subjects:
  • Disulfide Bonds
  • Escherichia Coli
  • Crystal Structure
  • Lactose
ispartof: Proceedings of the National Academy of Sciences of the United States of America, 2011, Vol.108(23), pp.9361-9366
description: Lactose permease of Escherichia coli (LacY) with a single-Cys residue in place of A122 (helix IV) transports galactopyranosides and is specifically inactivated by methanethiosulfonyl-galactopyranosides (MTS-gal), which behave as unique suicide substrates. In order to study the mechanism of inactivation more precisely, we solved the structure of single-Cys122 LacY in complex with covalently bound MTS-gal. This structure exhibits an inward-facing conformation similar to that observed previously with a slight narrowing of the cytoplasmic cavity. MTS-gal is bound covalently, forming a disulfide bond with C122 and positioned between R144 and W151. E269, a residue essential for binding, coordinates the C-4 hydroxyl of the galactopyranoside moiety. The location of the sugar is in accord with many biochemical studies. ; p. 9361-9366.
language: eng
source:
identifier: ISSN: 0027-8424
fulltext: fulltext
issn:
  • 00278424
  • 0027-8424
url: Link


@attributes
ID1591676771
RANK0.07
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
LOCALfalse
PrimoNMBib
record
control
sourcerecordidUS201600192405
sourceidfaoagris
recordidTN_faoagrisUS201600192405
sourcesystemPC
pqid871380957
galeid259679184
display
typearticle
titleCrystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition
creatorChaptal , Vincent ; Kwon , Seunghyug ; Sawaya , Michael R. ; Guan , Lan ; Kaback , H. Ronald ; Abramson , Jeff
publisherNational Academy of Sciences
creationdate2011
ispartofProceedings of the National Academy of Sciences of the United States of America, 2011, Vol.108(23), pp.9361-9366
identifierISSN: 0027-8424
subjectDisulfide Bonds ; Escherichia Coli ; Crystal Structure ; Lactose
descriptionLactose permease of Escherichia coli (LacY) with a single-Cys residue in place of A122 (helix IV) transports galactopyranosides and is specifically inactivated by methanethiosulfonyl-galactopyranosides (MTS-gal), which behave as unique suicide substrates. In order to study the mechanism of inactivation more precisely, we solved the structure of single-Cys122 LacY in complex with covalently bound MTS-gal. This structure exhibits an inward-facing conformation similar to that observed previously with a slight narrowing of the cytoplasmic cavity. MTS-gal is bound covalently, forming a disulfide bond with C122 and positioned between R144 and W151. E269, a residue essential for binding, coordinates the C-4 hydroxyl of the galactopyranoside moiety. The location of the sugar is in accord with many biochemical studies. ; p. 9361-9366.
languageeng
source
version10
lds50peer_reviewed
links
openurl$$Topenurl_article
linktorsrc$$Uhttp://dx.doi.org/10.1073/pnas.1105687108$$EView_full_text_(authentication_may_be_required)
openurlfulltext$$Topenurlfull_article
search
creatorcontrib
0Chaptal , Vincent
1Kwon , Seunghyug
2Sawaya , Michael R.
3Guan , Lan
4Kaback , H. Ronald
5Abramson , Jeff
titleCrystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition
descriptionLactose permease of Escherichia coli (LacY) with a single-Cys residue in place of A122 (helix IV) transports galactopyranosides and is specifically inactivated by methanethiosulfonyl-galactopyranosides (MTS-gal), which behave as unique suicide substrates. In order to study the mechanism of inactivation more precisely, we solved the structure of single-Cys122 LacY in complex with covalently bound MTS-gal. This structure exhibits an inward-facing conformation similar to that observed previously with a slight narrowing of the cytoplasmic cavity. MTS-gal is bound covalently, forming a disulfide bond with C122 and positioned between R144 and W151. E269, a residue essential for binding, coordinates the C-4 hydroxyl of the galactopyranoside moiety. The location of the sugar is in accord with many biochemical studies. ; p. 9361-9366.
subject
0Disulfide Bonds
1Escherichia Coli
2Crystal Structure
3Lactose
general
0English
1National Academy of Sciences
2AGRIS (United Nations, Food and Agriculture Organization)
sourceidfaoagris
recordidfaoagrisUS201600192405
rsrctypeconference_proceeding
creationdate2011
addtitleProceedings of the National Academy of Sciences of the United States of America
searchscope
0faoagris
1faoagris_lr
scope
0faoagris
1faoagris_lr
alttitleCrystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition
issn
000278424
10027-8424
lsr30VSR-Enriched:[eissn, doi, pqid, date, galeid]
sort
titleCrystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition
authorChaptal , Vincent ; Kwon , Seunghyug ; Sawaya , Michael R. ; Guan , Lan ; Kaback , H. Ronald ; Abramson , Jeff
creationdate20110000
facets
frbrgroupid6432123940214267107
frbrtype5
newrecords20170103
languageeng
creationdate2011
topic
0Disulfide Bonds
1Escherichia Coli
2Crystal Structure
3Lactose
collectionAGRIS (United Nations, Food and Agriculture Organization)
prefilterconference_proceedings
rsrctypeconference_proceedings
creatorcontrib
0Chaptal , Vincent
1Kwon , Seunghyug
2Sawaya , Michael R.
3Guan , Lan
4Kaback , H. Ronald
5Abramson , Jeff
jtitleProceedings of the National Academy of Sciences of the United States of America
toplevelpeer_reviewed
delivery
delcategoryRemote Search Resource
fulltextfulltext
addata
au
0Chaptal, Vincent
1Kwon, Seunghyug
2Sawaya, Michael R.
3Guan, Lan
4Kaback, H. Ronald
5Abramson, Jeff
atitleCrystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition
jtitleProceedings of the National Academy of Sciences of the United States of America
addtitleCrystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition
risdate2011
volume108
issue23
spage9361
epage9366
pages9361-9366
issn0027-8424
abstractLactose permease of Escherichia coli (LacY) with a single-Cys residue in place of A122 (helix IV) transports galactopyranosides and is specifically inactivated by methanethiosulfonyl-galactopyranosides (MTS-gal), which behave as unique suicide substrates. In order to study the mechanism of inactivation more precisely, we solved the structure of single-Cys122 LacY in complex with covalently bound MTS-gal. This structure exhibits an inward-facing conformation similar to that observed previously with a slight narrowing of the cytoplasmic cavity. MTS-gal is bound covalently, forming a disulfide bond with C122 and positioned between R144 and W151. E269, a residue essential for binding, coordinates the C-4 hydroxyl of the galactopyranoside moiety. The location of the sugar is in accord with many biochemical studies.
pubNational Academy of Sciences
doi10.1073/pnas.1105687108
eissn10916490
date2011-06-07
genrearticle
formatjournal
ristypeJOUR