DSpace UNL

RUN >
Instituto de Tecnologia Química e Biológica (ITQB) >
ITQB R&D Units >
ITQB: Biology >
ITQB: Bacterial Signalling >
ITQB: BS - Artigos em revista nacional com arbitragem científica >

Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/5860

Título: The Crystal Structure of the Escherichia coli Autoinducer-2 Processing Protein LsrF
Autor: Diaz, Z.
Xavier, K. B.
Miller, S. T.
Issue Date: 1-Jan-2009
Editora: Public Library of Science
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.
Descrição: PLOS ONE, 4(8):ARTe6820
URI: http://hdl.handle.net/10362/5860
ISSN: 1932-6203
Appears in Collections:ITQB: BS - Artigos em revista nacional com arbitragem científica

Files in This Item:

File Description SizeFormat
01407.pdf633,5 kBAdobe PDFView/Open

Please give feedback about this item
Statistics
FacebookTwitterDeliciousLinkedInDiggGoogle BookmarksMySpaceOrkut
Formato BibTex mendeley Endnote Logotipo do DeGóis 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

 

Universidade Nova de Lisboa  - Feedback
Promotores do RCAAP   Financiadores do RCAAP

Fundação para a Ciência e a Tecnologia Universidade do Minho   Governo Português Ministério da Educação e Ciência PO Sociedade do Conhecimento (POSC) Portal oficial da União Europeia