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2yfa

From Proteopedia

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Current revision

X-ray structure of McpS ligand binding domain in complex with malate

Structural highlights

2yfa is a 2 chain structure with sequence from Pseudomonas putida KT2440. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MCPS_PSEPK Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. McpS is a specific chemoreceptor for 6 tricarboxylic acid (TCA) cycle intermediates (succinate, fumarate, malate, oxaloacetate, citrate and isocitrate), butyrate and acetate. Malate, succinate, fumarate and oxaloacetate cause the strongest chemotactic response.^[1] ^[2]

Publication Abstract from PubMed

Chemoreceptor-based signaling is a central mechanism in bacterial signal transduction. Receptors are classified according to the size of their ligand-binding region. The well-studied cluster I proteins have a 100- to 150-residue ligand-binding region that contains a single site for chemoattractant recognition. Cluster II receptors, which contain a 220- to 300-residue ligand-binding region and which are almost as abundant as cluster I receptors, remain largely uncharacterized. Here, we report high-resolution structures of the ligand-binding region of the cluster II McpS chemotaxis receptor (McpS-LBR) of Pseudomonas putida KT2440 in complex with different chemoattractants. The structure of McpS-LBR represents a small-molecule binding domain composed of two modules, each able to bind different signal molecules. Malate and succinate were found to bind to the membrane-proximal module, whereas acetate binds to the membrane-distal module. A structural alignment of the two modules revealed that the ligand-binding sites could be superimposed and that amino acids involved in ligand recognition are conserved in both binding sites. Ligand binding to both modules was shown to trigger chemotactic responses. Further analysis showed that McpS-like receptors were found in different classes of proteobacteria, indicating that this mode of response to different carbon sources may be universally distributed. The physiological relevance of the McpS architecture may lie in its capacity to respond with high sensitivity to the preferred carbon sources malate and succinate and, at the same time, mediate lower sensitivity responses to the less preferred but very abundant carbon source acetate.

Evidence for chemoreceptors with bimodular ligand-binding regions harboring two signal-binding sites.,Pineda-Molina E, Reyes-Darias JA, Lacal J, Ramos JL, Garcia-Ruiz JM, Gavira JA, Krell T Proc Natl Acad Sci U S A. 2012 Nov 13;109(46):18926-31. doi:, 10.1073/pnas.1201400109. Epub 2012 Oct 29. PMID:23112148^[3]

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

References

↑ Lacal J, Alfonso C, Liu X, Parales RE, Morel B, Conejero-Lara F, Rivas G, Duque E, Ramos JL, Krell T. Identification of a chemoreceptor for tricarboxylic acid cycle intermediates: differential chemotactic response towards receptor ligands. J Biol Chem. 2010 Jul 23;285(30):23126-36. PMID:20498372 doi:10.1074/jbc.M110.110403
↑ Lacal J, García-Fontana C, Callejo-García C, Ramos JL, Krell T. Physiologically relevant divalent cations modulate citrate recognition by the McpS chemoreceptor. J Mol Recognit. 2011 Mar-Apr;24(2):378-85. PMID:21360620 doi:10.1002/jmr.1101
↑ Pineda-Molina E, Reyes-Darias JA, Lacal J, Ramos JL, Garcia-Ruiz JM, Gavira JA, Krell T. Evidence for chemoreceptors with bimodular ligand-binding regions harboring two signal-binding sites. Proc Natl Acad Sci U S A. 2012 Nov 13;109(46):18926-31. doi:, 10.1073/pnas.1201400109. Epub 2012 Oct 29. PMID:23112148 doi:10.1073/pnas.1201400109

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2yfa"

Categories: Large Structures | Pseudomonas putida KT2440 | Gavira JA | Krell T | Pineda-Molina E

@@ Line 3: / Line 3: @@
 <StructureSection load='2yfa' size='340' side='right'caption='[[2yfa]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2yfa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Psepk Psepk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YFA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2yfa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_KT2440 Pseudomonas putida KT2440]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YFA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=LMR:(2S)-2-HYDROXYBUTANEDIOIC+ACID'>LMR</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2yfb|2yfb]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=LMR:(2S)-2-HYDROXYBUTANEDIOIC+ACID'>LMR</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2yfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yfa OCA], [https://pdbe.org/2yfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yfa RCSB], [https://www.ebi.ac.uk/pdbsum/2yfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yfa ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/MCPS_PSEPK MCPS_PSEPK] Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. McpS is a specific chemoreceptor for 6 tricarboxylic acid (TCA) cycle intermediates (succinate, fumarate, malate, oxaloacetate, citrate and isocitrate), butyrate and acetate. Malate, succinate, fumarate and oxaloacetate cause the strongest chemotactic response.<ref>PMID:20498372</ref> <ref>PMID:21360620</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 24: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Psepk]]
+[[Category: Pseudomonas putida KT2440]]
-[[Category: Gavira, J A]]
+[[Category: Gavira JA]]
-[[Category: Krell, T]]
+[[Category: Krell T]]
-[[Category: Pineda-Molina, E]]
+[[Category: Pineda-Molina E]]
-[[Category: Chemoreceptor]]
-[[Category: Chemotaxis]]
-[[Category: Receptor]]

2yfa

From Proteopedia

Current revision

X-ray structure of McpS ligand binding domain in complex with malate

Structural highlights

Function

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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