schliessen

Filtern

 

Bibliotheken

Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase.

Legionella pneumophila is an opportunistic intracellular pathogen that causes sporadic and epidemic cases of Legionnaires' disease. Emerging data suggest that Legionella infection involves the subversion of host phosphoinositide (PI) metabolism. However, how this bacterium actively manipulates PI li... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America August 21, 2012, Vol.109(34), pp.13567-13572
Main Author: Hsu, Fosheng
Other Authors: Zhu, Wenhan , Brennan, Lucy , Tao, Lili , Luo, Zhao-Qing , Mao, Yuxin
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1207903109
Link: http://search.proquest.com/docview/1034808175/?pq-origsite=primo
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: proquest1034808175
title: Structural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase.
format: Article
creator:
  • Hsu, Fosheng
  • Zhu, Wenhan
  • Brennan, Lucy
  • Tao, Lili
  • Luo, Zhao-Qing
  • Mao, Yuxin
subjects:
  • Bacterial Proteins–Chemistry
  • Catalysis–Methods
  • Catalytic Domain–Enzymology
  • Crystallography, X-Ray–Chemistry
  • Hydrolysis–Metabolism
  • Legionella Pneumophila–Chemistry
  • Lipids–Chemistry
  • Molecular Conformation–Chemistry
  • Oxidation-Reduction–Chemistry
  • Phagocytosis–Chemistry
  • Phagosomes–Chemistry
  • Phosphatidylinositols–Chemistry
  • Phosphoric Monoester Hydrolases–Chemistry
  • Protein Structure, Tertiary–Chemistry
  • Substrate Specificity–Chemistry
  • Bacterial Proteins
  • Lipids
  • Phosphatidylinositols
  • Polyphosphoinositide Phosphatase
  • Phosphoric Monoester Hydrolases
ispartof: Proceedings of the National Academy of Sciences of the United States of America, August 21, 2012, Vol.109(34), pp.13567-13572
description: Legionella pneumophila is an opportunistic intracellular pathogen that causes sporadic and epidemic cases of Legionnaires' disease. Emerging data suggest that Legionella infection involves the subversion of host phosphoinositide (PI) metabolism. However, how this bacterium actively manipulates PI lipids to benefit its infection is still an enigma. Here, we report that the L. pneumophila virulence factor SidF is a phosphatidylinositol polyphosphate 3-phosphatase that specifically hydrolyzes the D3 phosphate of PI(3,4)[P.sub.2] and PI(3,4,5)[P.sub.3]. This activity is necessary for anchoring of PI(4)P-binding effectors to bacterial phagosomes. Crystal structures of SidF and its complex with its substrate PI(3,4)[P.sub.2] reveal striking conformational rearrangement of residues at the catalytic site to form a cationic pocket that specifically accommodates the D4 phosphate group of the substrate. Thus, our findings unveil a unique Legionella PI phosphatase essential for the establishment of lipid identity of bacterial phagosomes. phosphoinositide signaling | phagocytosis | membrane trafficking | type IV secretion system | virulence factor www.pnas.org/cgi/doi/10.1073/pnas.1207903109
language: eng
source:
identifier: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1207903109
fulltext: fulltext
issn:
  • 10916490
  • 1091-6490
url: Link


@attributes
ID361536740
RANK0.07
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
LOCALfalse
PrimoNMBib
record
control
sourcerecordid1034808175
sourceidproquest
recordidTN_proquest1034808175
sourcesystemPC
pqid1034808175
galeid301966411
display
typearticle
titleStructural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase.
creatorHsu, Fosheng ; Zhu, Wenhan ; Brennan, Lucy ; Tao, Lili ; Luo, Zhao-Qing ; Mao, Yuxin
contributorHsu, Fosheng (correspondence author) ; Hsu, Fosheng (record owner)
ispartofProceedings of the National Academy of Sciences of the United States of America, August 21, 2012, Vol.109(34), pp.13567-13572
identifierE-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1207903109
subjectBacterial Proteins–Chemistry ; Catalysis–Methods ; Catalytic Domain–Enzymology ; Crystallography, X-Ray–Chemistry ; Hydrolysis–Metabolism ; Legionella Pneumophila–Chemistry ; Lipids–Chemistry ; Molecular Conformation–Chemistry ; Oxidation-Reduction–Chemistry ; Phagocytosis–Chemistry ; Phagosomes–Chemistry ; Phosphatidylinositols–Chemistry ; Phosphoric Monoester Hydrolases–Chemistry ; Protein Structure, Tertiary–Chemistry ; Substrate Specificity–Chemistry ; Bacterial Proteins ; Lipids ; Phosphatidylinositols ; Polyphosphoinositide Phosphatase ; Phosphoric Monoester Hydrolases
languageeng
source
descriptionLegionella pneumophila is an opportunistic intracellular pathogen that causes sporadic and epidemic cases of Legionnaires' disease. Emerging data suggest that Legionella infection involves the subversion of host phosphoinositide (PI) metabolism. However, how this bacterium actively manipulates PI lipids to benefit its infection is still an enigma. Here, we report that the L. pneumophila virulence factor SidF is a phosphatidylinositol polyphosphate 3-phosphatase that specifically hydrolyzes the D3 phosphate of PI(3,4)[P.sub.2] and PI(3,4,5)[P.sub.3]. This activity is necessary for anchoring of PI(4)P-binding effectors to bacterial phagosomes. Crystal structures of SidF and its complex with its substrate PI(3,4)[P.sub.2] reveal striking conformational rearrangement of residues at the catalytic site to form a cationic pocket that specifically accommodates the D4 phosphate group of the substrate. Thus, our findings unveil a unique Legionella PI phosphatase essential for the establishment of lipid identity of bacterial phagosomes. phosphoinositide signaling | phagocytosis | membrane trafficking | type IV secretion system | virulence factor www.pnas.org/cgi/doi/10.1073/pnas.1207903109
version10
lds50peer_reviewed
links
openurl$$Topenurl_article
openurlfulltext$$Topenurlfull_article
backlink$$Uhttp://search.proquest.com/docview/1034808175/?pq-origsite=primo$$EView_record_in_ProQuest_(subscribers_only)
search
creatorcontrib
0Hsu, Fosheng
1Zhu, Wenhan
2Brennan, Lucy
3Tao, Lili
4Luo, Zhao-Qing
5Mao, Yuxin
titleStructural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase.
subject
0Bacterial Proteins–Chemistry
1Catalysis–Methods
2Catalytic Domain–Enzymology
3Crystallography, X-Ray–Chemistry
4Hydrolysis–Metabolism
5Legionella Pneumophila–Chemistry
6Lipids–Chemistry
7Molecular Conformation–Chemistry
8Oxidation-Reduction–Chemistry
9Phagocytosis–Chemistry
10Phagosomes–Chemistry...
114FYE
124FYF
134FYG
14PDB
general
0English
110.1073/pnas.1207903109
2MEDLINE (ProQuest)
3ProQuest Biological Science Collection
4ProQuest Natural Science Collection
5ProQuest SciTech Collection
6Biological Science Database
7Natural Science Collection
8SciTech Premium Collection
9Health Research Premium Collection
10Health Research Premium Collection (Alumni edition)
11Biological Science Index (ProQuest)
sourceidproquest
recordidproquest1034808175
issn
010916490
11091-6490
rsrctypearticle
creationdate2012
addtitleProceedings of the National Academy of Sciences of the United States of America
searchscope
01007527
11007944
21009130
310000004
410000038
510000050
610000120
710000159
810000238
910000253
1010000260
1110000270
1210000271
1310000302
1410000350
15proquest
scope
01007527
11007944
21009130
310000004
410000038
510000050
610000120
710000159
810000238
910000253
1010000260
1110000270
1210000271
1310000302
1410000350
15proquest
lsr43
01007527false
11007944false
21009130false
310000004false
410000038false
510000050false
610000120false
710000159false
810000238false
910000253false
1010000260false
1110000270false
1210000271false
1310000302false
1410000350false
contributorHsu, Fosheng
startdate20120821
enddate20120821
citationpf 13567 pt 13572 vol 109 issue 34
lsr30VSR-Enriched:[description, pqid, galeid, issn]
sort
titleStructural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase.
authorHsu, Fosheng ; Zhu, Wenhan ; Brennan, Lucy ; Tao, Lili ; Luo, Zhao-Qing ; Mao, Yuxin
creationdate20120821
lso0120120821
facets
frbrgroupid7527539713778952213
frbrtype5
newrecords20181218
languageeng
creationdate2012
topic
0Bacterial Proteins–Chemistry
1Catalysis–Methods
2Catalytic Domain–Enzymology
3Crystallography, X-Ray–Chemistry
4Hydrolysis–Metabolism
5Legionella Pneumophila–Chemistry
6Lipids–Chemistry
7Molecular Conformation–Chemistry
8Oxidation-Reduction–Chemistry
9Phagocytosis–Chemistry
10Phagosomes–Chemistry...
collection
0MEDLINE (ProQuest)
1ProQuest Biological Science Collection
2ProQuest Natural Science Collection
3ProQuest SciTech Collection
4Biological Science Database
5Natural Science Collection
6SciTech Premium Collection
7Health Research Premium Collection
8Health Research Premium Collection (Alumni edition)
9Biological Science Index (ProQuest)
prefilterarticles
rsrctypearticles
creatorcontrib
0Hsu, Fosheng
1Zhu, Wenhan
2Brennan, Lucy
3Tao, Lili
4Luo, Zhao-Qing
5Mao, Yuxin
jtitleProceedings of the National Academy of Sciences of the United States of America
toplevelpeer_reviewed
delivery
delcategoryRemote Search Resource
fulltextfulltext
addata
aulast
0Hsu
1Zhu
2Brennan
3Tao
4Luo
5Mao
aufirst
0Fosheng
1Wenhan
2Lucy
3Lili
4Zhao-Qing
5Yuxin
au
0Hsu, Fosheng
1Zhu, Wenhan
2Brennan, Lucy
3Tao, Lili
4Luo, Zhao-Qing
5Mao, Yuxin
addauHsu, Fosheng
atitleStructural basis for substrate recognition by a unique Legionella phosphoinositide phosphatase.
jtitleProceedings of the National Academy of Sciences of the United States of America
risdate20120821
volume109
issue34
spage13567
epage13572
pages13567-13572
eissn1091-6490
formatjournal
genrearticle
ristypeJOUR
doi10.1073/pnas.1207903109
urlhttp://search.proquest.com/docview/1034808175/
issn00278424
date2012-08-21