5ya1

From Proteopedia

(Difference between revisions)

Revision as of 09:14, 21 October 2020

crystal structure of LsrK-HPr complex with ATP

Structural highlights

5ya1 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Activity:	Autoinducer-2 kinase, with EC number 2.7.1.189
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] [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).

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^[4]

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

References

↑ 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
↑ 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
↑ 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
↑ Ha JH, Hauk P, Cho K, Eo Y, Ma X, Stephens K, Cha S, Jeong M, Suh JY, Sintim HO, Bentley WE, Ryu KS. Evidence of link between quorum sensing and sugar metabolism in Escherichia coli revealed via cocrystal structures of LsrK and HPr. Sci Adv. 2018 Jun 1;4(6):eaar7063. doi: 10.1126/sciadv.aar7063. eCollection 2018 , Jun. PMID:29868643 doi:http://dx.doi.org/10.1126/sciadv.aar7063

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ya1"

@@ Line 1: / Line 1: @@
 ==crystal structure of LsrK-HPr complex with ATP==
-<StructureSection load='5ya1' size='340' side='right' caption='[[5ya1]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='5ya1' size='340' side='right'caption='[[5ya1]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ya1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YA1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YA1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ya1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YA1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YA1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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='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=5ya1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ya1 OCA], [http://pdbe.org/5ya1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ya1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ya1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ya1 ProSAT]</span></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=5ya1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ya1 OCA], [http://pdbe.org/5ya1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ya1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ya1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ya1 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 5ya1" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
 == References ==
 <references/>
@@ Line 24: / Line 27: @@
 </StructureSection>
 [[Category: Autoinducer-2 kinase]]
+[[Category: Large Structures]]
 [[Category: Ha, J H]]
 [[Category: Ryu, K S]]
 [[Category: Atp binding]]
 [[Category: Structural protein]]

5ya1

From Proteopedia

Revision as of 09:14, 21 October 2020

crystal structure of LsrK-HPr complex with ATP

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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