5ya2: Difference between revisions

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New page: '''Unreleased structure''' The entry 5ya2 is ON HOLD until Paper Publication Authors: Ryu, K.S., Ha, J.H. Description: Crystal structure of LsrK-HPr complex with ADP [[Category: Unrele...
 
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'''Unreleased structure'''


The entry 5ya2 is ON HOLD  until Paper Publication
==Crystal structure of LsrK-HPr complex with ADP==
<StructureSection load='5ya2' size='340' side='right'caption='[[5ya2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<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='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='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'>[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>
== Function ==
[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>


Authors: Ryu, K.S., Ha, J.H.
==See Also==
 
*[[Phosphocarrier protein HPr 3D structures|Phosphocarrier protein HPr 3D structures]]
Description: Crystal structure of LsrK-HPr complex with ADP
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Ha, J.H]]
__TOC__
[[Category: Ryu, K.S]]
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Ha JH]]
[[Category: Ryu KS]]

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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