1vje

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[[Image:1vje.gif|left|200px]]<br /><applet load="1vje" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1vje.gif|left|200px]]
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caption="1vje, resolution 1.64&Aring;" />
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'''Crystal structure of a autoinducer-2 synthesis protein with bound selenomethionine'''<br />
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{{Structure
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|PDB= 1vje |SIZE=350|CAPTION= <scene name='initialview01'>1vje</scene>, resolution 1.64&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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|ACTIVITY=
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|GENE= LUXS, DR2387 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1299 Deinococcus radiodurans])
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}}
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'''Crystal structure of a autoinducer-2 synthesis protein with bound selenomethionine'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1VJE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=MSE:'>MSE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJE OCA].
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1VJE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJE OCA].
==Reference==
==Reference==
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A structural genomics approach to the study of quorum sensing: crystal structures of three LuxS orthologs., Lewis HA, Furlong EB, Laubert B, Eroshkina GA, Batiyenko Y, Adams JM, Bergseid MG, Marsh CD, Peat TS, Sanderson WE, Sauder JM, Buchanan SG, Structure. 2001 Jun;9(6):527-37. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11435117 11435117]
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A structural genomics approach to the study of quorum sensing: crystal structures of three LuxS orthologs., Lewis HA, Furlong EB, Laubert B, Eroshkina GA, Batiyenko Y, Adams JM, Bergseid MG, Marsh CD, Peat TS, Sanderson WE, Sauder JM, Buchanan SG, Structure. 2001 Jun;9(6):527-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11435117 11435117]
[[Category: Deinococcus radiodurans]]
[[Category: Deinococcus radiodurans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: MSE]]
[[Category: MSE]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:35:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:46:26 2008''

Revision as of 12:46, 20 March 2008


PDB ID 1vje

Drag the structure with the mouse to rotate
, resolution 1.64Å
Ligands: and
Gene: LUXS, DR2387 (Deinococcus radiodurans)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of a autoinducer-2 synthesis protein with bound selenomethionine


Overview

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.

About this Structure

1VJE is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.

Reference

A structural genomics approach to the study of quorum sensing: crystal structures of three LuxS orthologs., Lewis HA, Furlong EB, Laubert B, Eroshkina GA, Batiyenko Y, Adams JM, Bergseid MG, Marsh CD, Peat TS, Sanderson WE, Sauder JM, Buchanan SG, Structure. 2001 Jun;9(6):527-37. PMID:11435117

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