دورية أكاديمية

Research Article 711 Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA

التفاصيل البيبلوغرافية
العنوان: Research Article 711 Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA
المؤلفون: Jacek Lubkowski, Frank Hennecke, Andreas Plückthun, Er Wlodawer
المساهمون: The Pennsylvania State University CiteSeerX Archives
المصدر: http://mcl1.ncifcrf.gov/wlo_pubs/180.pdfTest.
سنة النشر: 1999
المجموعة: CiteSeerX
مصطلحات موضوعية: Key words, phage display, phage infection, protein fusion, protein structure, structure refinement
الوصف: Background: Infection of male Escherichia coli cells by filamentous Ff bacteriophages (M13, fd, and f1) involves interaction of the phage minor coat gene 3 protein (g3p) with the bacterial F pilus (primary receptor), and subsequently with the integral membrane protein TolA (coreceptor). G3p consists of three domains (N1, N2, and CT). The N2 domain interacts with the F pilus, whereas the N1 domain — connected to N2 by a flexible glycine-rich linker and tightly interacting with it on the phage — forms a complex with the C-terminal domain of TolA at later stages of the infection process. Results: The crystal structure of the complex between g3p N1 and TolA D3 was obtained by fusing these domains with a long flexible linker, which was not visible in the structure, indicating its very high disorder and presumably a lack of interference with the formation of the complex. The interface between both domains, corresponding to ~1768 Å 2 of buried molecular surface, is clearly defined. Despite the lack of topological similarity between TolA D3 and g3p N2, both domains interact with the same region of the g3p N1 domain. The fold of
نوع الوثيقة: text
وصف الملف: application/pdf
اللغة: English
العلاقة: http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.334.4501Test; http://mcl1.ncifcrf.gov/wlo_pubs/180.pdfTest
الإتاحة: http://mcl1.ncifcrf.gov/wlo_pubs/180.pdfTest
حقوق: Metadata may be used without restrictions as long as the oai identifier remains attached to it.
رقم الانضمام: edsbas.751CD2A4
قاعدة البيانات: BASE