5ya2: Difference between revisions

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<StructureSection load='5ya2' size='340' side='right'caption='[[5ya2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='5ya2' size='340' side='right'caption='[[5ya2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ya2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YA2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YA2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ya2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YA2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.701&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Autoinducer-2_kinase Autoinducer-2 kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.189 2.7.1.189] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ya2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ya2 OCA], [http://pdbe.org/5ya2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ya2 RCSB], [http://www.ebi.ac.uk/pdbsum/5ya2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ya2 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=5ya2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ya2 OCA], [https://pdbe.org/5ya2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ya2 RCSB], [https://www.ebi.ac.uk/pdbsum/5ya2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ya2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/LSRK_ECOLI LSRK_ECOLI]] Catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. Phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. Required for the regulation of the lsr operon and many other genes.<ref>PMID:15601708</ref> <ref>PMID:17557827</ref> <ref>PMID:20025244</ref>  [[http://www.uniprot.org/uniprot/PTHP_ECOLI PTHP_ECOLI]] General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III).
[https://www.uniprot.org/uniprot/LSRK_ECOLI LSRK_ECOLI] Catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. Phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. Required for the regulation of the lsr operon and many other genes.<ref>PMID:15601708</ref> <ref>PMID:17557827</ref> <ref>PMID:20025244</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Quorum sensing (QS), a bacterial process that regulates population-scale behavior, is mediated by small signaling molecules, called autoinducers (AIs), that are secreted and perceived, modulating a "collective" phenotype. Because the autoinducer AI-2 is secreted by a wide variety of bacterial species, its "perception" cues bacterial behavior. This response is mediated by the lsr (LuxS-regulated) operon that includes the AI-2 transporter LsrACDB and the kinase LsrK. We report that HPr, a phosphocarrier protein central to the sugar phosphotransferase system of Escherichia coli, copurifies with LsrK. Cocrystal structures of an LsrK/HPr complex were determined, and the effects of HPr and phosphorylated HPr on LsrK activity were assessed. LsrK activity is inhibited when bound to HPr, revealing new linkages between QS activity and sugar metabolism. These findings help shed new light on the abilities of bacteria to rapidly respond to changing nutrient levels at the population scale. They also suggest new means of manipulating QS activity among bacteria and within various niches.
 
Evidence of link between quorum sensing and sugar metabolism in Escherichia coli revealed via cocrystal structures of LsrK and HPr.,Ha JH, Hauk P, Cho K, Eo Y, Ma X, Stephens K, Cha S, Jeong M, Suh JY, Sintim HO, Bentley WE, Ryu KS Sci Adv. 2018 Jun 1;4(6):eaar7063. doi: 10.1126/sciadv.aar7063. eCollection 2018 , Jun. PMID:29868643<ref>PMID:29868643</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ya2" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Autoinducer-2 kinase]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ha, J H]]
[[Category: Ha JH]]
[[Category: Ryu, K S]]
[[Category: Ryu KS]]
[[Category: Adp binding]]
[[Category: Complex]]
[[Category: Hpr]]
[[Category: Lsrk]]
[[Category: Quorum sensing]]
[[Category: Structural protein]]

Latest revision as of 13:22, 27 March 2024

Crystal structure of LsrK-HPr complex with ADPCrystal structure of LsrK-HPr complex with ADP

Structural highlights

5ya2 is a 4 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.701Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LSRK_ECOLI Catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. Phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. Required for the regulation of the lsr operon and many other genes.[1] [2] [3]

See Also

References

  1. ↑ Xavier KB, Bassler BL. Regulation of uptake and processing of the quorum-sensing autoinducer AI-2 in Escherichia coli. J Bacteriol. 2005 Jan;187(1):238-48. PMID:15601708 doi:http://dx.doi.org/187/1/238
  2. ↑ Li J, Attila C, Wang L, Wood TK, Valdes JJ, Bentley WE. Quorum sensing in Escherichia coli is signaled by AI-2/LsrR: effects on small RNA and biofilm architecture. J Bacteriol. 2007 Aug;189(16):6011-20. Epub 2007 Jun 8. PMID:17557827 doi:http://dx.doi.org/JB.00014-07
  3. ↑ Roy V, Fernandes R, Tsao CY, Bentley WE. Cross species quorum quenching using a native AI-2 processing enzyme. ACS Chem Biol. 2010 Feb 19;5(2):223-32. doi: 10.1021/cb9002738. PMID:20025244 doi:http://dx.doi.org/10.1021/cb9002738

5ya2, resolution 2.70Å

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