4p2v: Difference between revisions

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'''Unreleased structure'''
==Structure of the AI-2 processing enzyme LsrF in complex with the product of the LsrG reaction P-HPD==
<StructureSection load='4p2v' size='340' side='right' caption='[[4p2v]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4p2v]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P2V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P2V FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=26T:(3R)-3-HYDROXY-2,4-DIOXOPENTYL+DIHYDROGEN+PHOSPHATE'>26T</scene><br>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4p2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p2v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p2v RCSB], [http://www.ebi.ac.uk/pdbsum/4p2v PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The quorum sensing signal autoinducer-2 (AI-2) regulates important bacterial behaviors, including biofilm formation and the production of virulence factors. Some bacteria, such as Escherichia coli, can quench the AI-2 signal produced by a variety of species present in the environment, and thus can influence AI-2-dependent bacterial behaviors. This process involves uptake of AI-2 via the Lsr transporter, followed by phosphorylation and consequent intracellular sequestration. Here we determine the metabolic fate of intracellular AI-2 by characterizing LsrF, the terminal protein in the Lsr AI-2 processing pathway. We identify the substrates of LsrF as 3-hydroxy-2,4-pentadione-5-phosphate (P-HPD, an isomer of AI-2-phosphate) and coenzyme A, determine the crystal structure of an LsrF catalytic mutant bound to P-HPD, and identify the reaction products. We show that LsrF catalyzes the transfer of an acetyl group from P-HPD to coenzyme A yielding dihydroxyacetone phosphate and acetyl-CoA, two key central metabolites. We further propose that LsrF, despite strong structural homology to aldolases, acts as a thiolase, an activity previously undescribed for this family of enzymes. With this work, we have fully characterized the biological pathway for AI-2 processing in E. coli, a pathway that can be used to quench AI-2 and control quorum-sensing-regulated bacterial behaviors.


The entry 4p2v is ON HOLD
LsrF, a coenzyme A-dependent thiolase, catalyzes the terminal step in processing the quorum sensing signal autoinducer-2.,Marques JC, Oh IK, Ly DC, Lamosa P, Ventura MR, Miller ST, Xavier KB Proc Natl Acad Sci U S A. 2014 Sep 15. pii: 201408691. PMID:25225400<ref>PMID:25225400</ref>


Authors: Miller, S.T., Oh, I.K., Xavier, K.B.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Structure of the AI-2 processing enzyme LsrF in complex with the product of the LsrG reaction P-HPD
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Miller, S T.]]
[[Category: Oh, I K.]]
[[Category: Xavier, K B.]]
[[Category: Lyase]]
[[Category: Thiolase]]
Retrieved from "https://proteopedia.org/4p2v"