000141270 001__ 141270
000141270 005__ 20250730151049.0
000141270 0247_ $$2pmid$$apmid:23188826
000141270 0247_ $$2pmc$$apmc:PMC3543004
000141270 0247_ $$2doi$$a10.1074/jbc.M112.432096
000141270 0247_ $$2ISSN$$a1083-351X
000141270 0247_ $$2ISSN$$a0021-9258
000141270 0247_ $$2WOS$$aWOS:000313570300042
000141270 0247_ $$2openalex$$aopenalex:W2000543721
000141270 037__ $$aPHPPUBDB-25356
000141270 041__ $$aeng
000141270 082__ $$a570
000141270 1001_ $$aVan der Meeren, R.
000141270 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000141270 245__ $$aNew insights into the assembly of bacterial secretins: structural studies of the periplasmic domain of XcpQ from Pseudomonas aeruginosa
000141270 260__ $$aBethesda, Md.$$bSoc.$$c2013
000141270 300__ $$a1214-1225
000141270 3367_ $$00$$2EndNote$$aJournal Article
000141270 3367_ $$2BibTeX$$aARTICLE
000141270 3367_ $$2DRIVER$$aarticle
000141270 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$mjournal
000141270 440_0 $$0PERI:(DE-600)1474604-9$$aJ. Biol. Chem.$$v288$$x0021-9258$$y2
000141270 500__ $$3Converted on 2013-05-30 09:55
000141270 500__ $$3Converted on 2013-06-21 19:21
000141270 520__ $$aThe type II secretion system is a multiprotein assembly spanning the inner and outer membranes in Gram-negative bacteria. It is found in almost all pathogenic bacteria where it contributes to virulence, host tissue colonization, and infection. The exoproteins are secreted across the outer membrane via a large translocation channel, the secretin, which typically adopts a dodecameric structure. These secretin channels have large periplasmic N-terminal domains that reach out into the periplasm for communication with the inner membrane platform and with a pseudopilus structure that spans the periplasm. Here we report the crystal structure of the N-terminal periplasmic domain of the secretin XcpQ from Pseudomonas aeruginosa, revealing a two-lobe dimeric assembly featuring parallel subunits engaging in well defined interactions at the tips of each lobe. We have employed structure-based engineering of disulfide bridges and native mass spectrometry to show that the periplasmic domain of XcpQ dimerizes in a concentration-dependent manner. Validation of these insights in the context of cellular full-length XcpQ and further evaluation of the functionality of disulfide-linked XcpQ establishes that the basic oligomerization unit of XcpQ is a dimer. This is consistent with the notion that the dodecameric secretin assembles as a hexamer of dimers to ensure correct projection of the N-terminal domains into the periplasm. Therefore, our studies provide a key conceptual advancement in understanding the assembly principles and dynamic function of type II secretion system secretins and challenge recent studies reporting monomers as the basic subunit of the secretin oligomer.
000141270 536__ $$0G:(DE-H253)POF2-D1.2-20130405$$aDORIS Beamline D1.2 (POF2-54G13)$$cPOF2-54G13$$fPOF II$$x0
000141270 588__ $$aDataset connected to Pubmed
000141270 650_2 $$2MeSH$$aAmino Acid Sequence
000141270 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000141270 650_2 $$2MeSH$$aBacterial Proteins: genetics
000141270 650_2 $$2MeSH$$aBacterial Proteins: metabolism
000141270 650_2 $$2MeSH$$aElectrophoresis, Polyacrylamide Gel
000141270 650_2 $$2MeSH$$aMass Spectrometry
000141270 650_2 $$2MeSH$$aMolecular Sequence Data
000141270 650_2 $$2MeSH$$aPeriplasm: metabolism
000141270 650_2 $$2MeSH$$aProtein Conformation
000141270 650_2 $$2MeSH$$aPseudomonas aeruginosa: metabolism
000141270 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000141270 650_2 $$2MeSH$$aRecombinant Proteins: genetics
000141270 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000141270 650_2 $$2MeSH$$aSecretin: metabolism
000141270 650_2 $$2MeSH$$aSequence Homology, Amino Acid
000141270 650_7 $$00$$2NLM Chemicals$$aBacterial Proteins
000141270 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000141270 650_7 $$01393-25-5$$2NLM Chemicals$$aSecretin
000141270 693__ $$0EXP:(DE-H253)D-D1.2-20150101$$1EXP:(DE-H253)DORISIII-20150101$$6EXP:(DE-H253)D-D1.2-20150101$$aDORIS III$$fDORIS Beamline D1.2$$x0
000141270 7001_ $$aWen, Y.
000141270 7001_ $$aVan Gelder, P.
000141270 7001_ $$aTommassen, J.
000141270 7001_ $$aDevreese, B.
000141270 7001_ $$aSavvides, S. N.
000141270 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M112.432096$$gVol. 288, p. 1214-1225$$p1214-1225$$q288<1214-1225$$tThe @journal of biological chemistry$$v288$$x0021-9258$$y2013
000141270 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3543004
000141270 909CO $$ooai:bib-pubdb1.desy.de:141270$$pVDB
000141270 9101_ $$0I:(DE-HGF)0$$aExternes Institut$$kExtern
000141270 9131_ $$0G:(DE-HGF)POF2-54G13$$1G:(DE-HGF)POF2-540$$2G:(DE-HGF)POF2-500$$3G:(DE-HGF)POF2$$4G:(DE-HGF)POF$$9G:(DE-H253)POF2-D1.2-20130405$$aDE-H253$$bStruktur der Materie$$lForschung mit Photonen, Neutronen, Ionen$$vDORIS III$$x0
000141270 9141_ $$y2013
000141270 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000141270 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aMedline
000141270 915__ $$0StatID:(DE-HGF)1$$2StatID$$aNo Author Disambiguation
000141270 920_1 $$iEuropean Molecular Biology Laboratory$$kEMBL
000141270 9201_ $$0I:(DE-H253)EMBL_-2012_-20130307$$kEMBL$$lEuropean Molecular Biology Laboratory$$x0
000141270 920__ $$k001
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000141270 980__ $$ajournal
000141270 980__ $$aI:(DE-H253)EMBL_-2012_-20130307
000141270 980__ $$aConvertedRecord