Oligomeric states of the Shigella translocator protein IpaB provide structural insights into formation of the type III secretion translocon.

Dickenson, Nicholas E; Choudhari, Shyamal P; Adam, Philip R; Kramer, Ryan M; Joshi, Sangeeta B; Middaugh, C Russell; Picking, Wendy L; Picking, William D

Dickenson, Nicholas E; Choudhari, Shyamal P; Adam, Philip R; Kramer, Ryan M; Joshi, Sangeeta B; Middaugh, C Russell; Picking, Wendy L; Picking, William D.

Affiliation

Dickenson NE; Department of Microbiology and Molecular Genetics, Oklahoma State University, Stillwater, Oklahoma 74078, USA.

Protein Sci ; 22(5): 614-27, 2013 May.

Article in En | MEDLINE | ID: mdl-23456854

Subject(s)

Bacterial Proteins/chemistry; Shigella flexneri/chemistry; Bacterial Proteins/metabolism; Dysentery, Bacillary/microbiology; Host-Pathogen Interactions; Humans; Liposomes/metabolism; Phospholipids/metabolism; Protein Conformation; Protein Multimerization; Protein Stability; Protein Transport; Shigella flexneri/metabolism; Shigella flexneri/physiology

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Shigella flexneri / Bacterial Proteins Limits: Humans Language: En Journal: Protein Sci Journal subject: BIOQUIMICA Year: 2013 Document type: Article Affiliation country: United States

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