Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.7/193
Título: The crystal structure of the Escherichia coli autoinducer-2 processing protein protein LsrF
Autor: Diaz, Z.
Xavier, KB.
Miller, ST.
Data: 28-Ago-2009
Editora: PLOS
Citação: Diaz, Z., Xavier, KB., Miller, ST. (2009). “The crystal structure of the Escherichia coli autoinducer-2 processing protein LsrF”. PLoS Genet. 4 (8): 1-10
Resumo: Many bacteria produce and respond to the quorum sensing signal autoinducer-2 (AI-2). Escherichia coli and Salmonella typhimurium are among the species with the lsr operon, an operon containing AI-2 transport and processing genes that are up regulated in response to AI-2. One of the Lsr proteins, LsrF, has been implicated in processing the phosphorylated form of AI-2. Here, we present the structure of LsrF, unliganded and in complex with two phospho-AI-2 analogues, ribose-5-phosphate and ribulose-5-phosphate. The crystal structure shows that LsrF is a decamer of (alpha beta)(8)-barrels that exhibit a previously unseen N-terminal domain swap and have high structural homology with aldolases that process phosphorylated sugars. Ligand binding sites and key catalytic residues are structurally conserved, strongly implicating LsrF as a class I aldolase.
URI: http://hdl.handle.net/10400.7/193
ISSN: 1932-6203
Aparece nas colecções:BS - Artigos

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