Publication
The crystal structure of the Escherichia coli autoinducer-2 processing protein protein LsrF
| dc.contributor.author | Diaz, Z. | |
| dc.contributor.author | Xavier, KB. | |
| dc.contributor.author | Miller, ST. | |
| dc.date.accessioned | 2010-08-12T09:08:48Z | |
| dc.date.available | 2010-08-12T09:08:48Z | |
| dc.date.issued | 2009-08-28 | |
| dc.description.abstract | 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. | |
| dc.identifier.citation | 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 | pt |
| dc.identifier.issn | 1932-6203 | |
| dc.identifier.uri | http://hdl.handle.net/10400.7/193 | |
| dc.language.iso | eng | pt |
| dc.publisher | PLOS | pt |
| dc.title | The crystal structure of the Escherichia coli autoinducer-2 processing protein protein LsrF | pt |
| dc.type | journal article | |
| dspace.entity.type | Publication | |
| oaire.citation.endPage | 10 | pt |
| oaire.citation.startPage | 1 | pt |
| oaire.citation.title | PLOS One | pt |
| rcaap.rights | openAccess | pt |
| rcaap.type | article | pt |