1j6w

From Proteopedia

(Difference between revisions)

Revision as of 07:16, 14 April 2021

CRYSTAL STRUCTURE OF HAEMOPHILUS INFLUENZAE LUXS

Structural highlights

1j6w is a 2 chain structure with sequence from "bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LUXS_HAEIN] Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1j6w"

@@ Line 3: / Line 3: @@
 <StructureSection load='1j6w' size='340' side='right'caption='[[1j6w]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1j6w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J6W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J6W FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1j6w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J6W FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j6w OCA], [http://pdbe.org/1j6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j6w RCSB], [http://www.ebi.ac.uk/pdbsum/1j6w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j6w ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1j6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j6w OCA], [https://pdbe.org/1j6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j6w RCSB], [https://www.ebi.ac.uk/pdbsum/1j6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j6w ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LUXS_HAEIN LUXS_HAEIN]] Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
+[[https://www.uniprot.org/uniprot/LUXS_HAEIN LUXS_HAEIN]] Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1j6w

From Proteopedia

Revision as of 07:16, 14 April 2021

CRYSTAL STRUCTURE OF HAEMOPHILUS INFLUENZAE LUXS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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