000321838 001__ 321838
000321838 005__ 20250730111849.0
000321838 0247_ $$2doi$$a10.1002/pro.2906
000321838 0247_ $$2ISSN$$a0961-8368
000321838 0247_ $$2ISSN$$a1469-896X
000321838 0247_ $$2WOS$$aWOS:000374686900005
000321838 0247_ $$2pmid$$apmid:26914207
000321838 0247_ $$2altmetric$$aaltmetric:6190789
000321838 0247_ $$2openalex$$aopenalex:W2299486352
000321838 037__ $$aPUBDB-2017-02769
000321838 041__ $$aEnglish
000321838 082__ $$a610
000321838 1001_ $$0P:(DE-H253)PIP1020745$$aMeriläinen, Gitte$$b0
000321838 245__ $$aThe extended structure of the periplasmic region of CdsD, a structural protein of the type III secretion system of Chlamydia trachomatis
000321838 260__ $$aHoboken, NJ$$bWiley$$c2016
000321838 3367_ $$2DRIVER$$aarticle
000321838 3367_ $$2DataCite$$aOutput Types/Journal article
000321838 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1498202790_11926
000321838 3367_ $$2BibTeX$$aARTICLE
000321838 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000321838 3367_ $$00$$2EndNote$$aJournal Article
000321838 520__ $$aThe type III secretion system (T3SS) is required for the virulence of many gram-negative bacterial human pathogens. It is composed of several structural proteins, forming the secretion needle and its basis, the basal body. In Chlamydia spp., the T3SS inner membrane ring (IM-ring) of the basal body is formed by the periplasmic part of CdsD (outer ring) and CdsJ (inner ring). Here we describe the crystal structure of the C-terminal, periplasmic part of CdsD, not including the last 60 residues. Two crystal forms were obtained, grown in three different crystallization conditions. In both crystal forms there is one molecule per asymmetric unit adopting a similar extended structure. The structures consist of three periplasmic domains (PDs) of similar αββαβ topology as seen also in the structures of the homologous PrgH (Salmonella typhimurium) and YscD (Yersinia enterocolitica). Only in the C2 crystal form, there is a C-terminal additional helix after the PD3 domain. The relative orientation of the three subsequent CdsD PD domains with respect to each other is more extended than in PrgH but less extended than in YscD. Small-angle X-ray scattering data show that also in solution this CdsD construct adopts the same elongated shape. In both crystal forms the CdsD molecules are packed in a parallel fashion, using translational crystallographic symmetry. The most extensive crystal contacts are preserved in both crystal forms, suggesting a possible mode of assembly of the CdsD periplasmic part into a 24-mer complex forming the outer ring of the IM-ring of the T3SS.
000321838 536__ $$0G:(DE-HGF)POF3-6G3$$a6G3 - PETRA III (POF3-622)$$cPOF3-622$$fPOF III$$x0
000321838 536__ $$0G:(EU-Grant)283570$$aBIOSTRUCT-X - Transnational access and enhancement of integrated Biological Structure determination at synchrotron X-ray radiation facilities (283570)$$c283570$$fFP7-INFRASTRUCTURES-2011-1$$x1
000321838 588__ $$aDataset connected to CrossRef
000321838 693__ $$0EXP:(DE-H253)P-P12-20150101$$1EXP:(DE-H253)PETRAIII-20150101$$6EXP:(DE-H253)P-P12-20150101$$aPETRA III$$fPETRA Beamline P12$$x0
000321838 7001_ $$aKoski, M. Kristian$$b1
000321838 7001_ $$0P:(DE-HGF)0$$aWierenga, Rik K.$$b2$$eCorresponding author
000321838 773__ $$0PERI:(DE-600)2000025-X$$a10.1002/pro.2906$$gVol. 25, no. 5, p. 987 - 998$$n5$$p987 - 998$$tProtein science$$v25$$x0961-8368$$y2016
000321838 8564_ $$uhttps://bib-pubdb1.desy.de/record/321838/files/Meril-inen_et_al-2016-Protein_Science.pdf$$yRestricted
000321838 8564_ $$uhttps://bib-pubdb1.desy.de/record/321838/files/Meril-inen_et_al-2016-Protein_Science.gif?subformat=icon$$xicon$$yRestricted
000321838 8564_ $$uhttps://bib-pubdb1.desy.de/record/321838/files/Meril-inen_et_al-2016-Protein_Science.jpg?subformat=icon-1440$$xicon-1440$$yRestricted
000321838 8564_ $$uhttps://bib-pubdb1.desy.de/record/321838/files/Meril-inen_et_al-2016-Protein_Science.jpg?subformat=icon-180$$xicon-180$$yRestricted
000321838 8564_ $$uhttps://bib-pubdb1.desy.de/record/321838/files/Meril-inen_et_al-2016-Protein_Science.jpg?subformat=icon-640$$xicon-640$$yRestricted
000321838 909CO $$ooai:bib-pubdb1.desy.de:321838$$pec_fundedresources$$pVDB$$popenaire
000321838 9101_ $$0I:(DE-HGF)0$$6P:(DE-H253)PIP1020745$$aExternes Institut$$b0$$kExtern
000321838 9131_ $$0G:(DE-HGF)POF3-622$$1G:(DE-HGF)POF3-620$$2G:(DE-HGF)POF3-600$$3G:(DE-HGF)POF3$$4G:(DE-HGF)POF$$9G:(DE-HGF)POF3-6G3$$aDE-HGF$$bForschungsbereich Materie$$lVon Materie zu Materialien und Leben$$vFacility topic: Research on Matter with Brilliant Light Sources$$x0
000321838 9141_ $$y2016
000321838 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bPROTEIN SCI : 2015
000321838 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000321838 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000321838 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000321838 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000321838 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000321838 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000321838 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000321838 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences
000321838 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000321838 915__ $$0StatID:(DE-HGF)9900$$2StatID$$aIF < 5
000321838 9201_ $$0I:(DE-H253)EMBL-20120731$$kEMBL$$lEMBL$$x0
000321838 9201_ $$0I:(DE-H253)EMBL-User-20120814$$kEMBL-User$$lEMBL-User$$x1
000321838 980__ $$ajournal
000321838 980__ $$aVDB
000321838 980__ $$aI:(DE-H253)EMBL-20120731
000321838 980__ $$aI:(DE-H253)EMBL-User-20120814
000321838 980__ $$aUNRESTRICTED