1inn: Difference between revisions

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[[Image:1inn.jpg|left|200px]]
{{Seed}}
[[Image:1inn.png|left|200px]]


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{{STRUCTURE_1inn|  PDB=1inn  |  SCENE=  }}  
{{STRUCTURE_1inn|  PDB=1inn  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF D. RADIODURANS LUXS, P21'''
===CRYSTAL STRUCTURE OF D. RADIODURANS LUXS, P21===




==Overview==
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BACKGROUND: Quorum sensing is the mechanism by which bacteria control gene expression in response to cell density. Two major quorum-sensing systems have been identified, system 1 and system 2, each with a characteristic signaling molecule (autoinducer-1, or AI-1, in the case of system 1, and AI-2 in system 2). The luxS gene is required for the AI-2 system of quorum sensing. LuxS and AI-2 have been described in both Gram-negative and Gram-positive bacterial species and have been shown to be involved in the expression of virulence genes in several pathogens. RESULTS: The structure of the LuxS protein from three different bacterial species with resolutions ranging from 1.8 A to 2.4 A has been solved using an X-ray crystallographic structural genomics approach. The structure of LuxS reported here is seen to have a new alpha-beta fold. In all structures, an equivalent homodimer is observed. A metal ion identified as zinc was seen bound to a Cys-His-His triad. Methionine was found bound to the protein near the metal and at the dimer interface. CONCLUSIONS: These structures provide support for a hypothesis that explains the in vivo action of LuxS. Specifically, acting as a homodimer, the protein binds a methionine analog, S-ribosylhomocysteine (SRH). The zinc atom is in position to cleave the ribose ring in a step along the synthesis pathway of AI-2.
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{{ABSTRACT_PUBMED_11435117}}


==About this Structure==
==About this Structure==
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[[Category: Sanderson, W E.]]
[[Category: Sanderson, W E.]]
[[Category: Alpha-beta fold]]
[[Category: Alpha-beta fold]]
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