5xlx

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Current revision (10:19, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5xlx' size='340' side='right'caption='[[5xlx]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
<StructureSection load='5xlx' size='340' side='right'caption='[[5xlx]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5xlx]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XLX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XLX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5xlx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XLX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.969&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-glutamate_O-methyltransferase Protein-glutamate O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.80 2.1.1.80] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5xlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xlx OCA], [http://pdbe.org/5xlx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xlx RCSB], [http://www.ebi.ac.uk/pdbsum/5xlx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xlx ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xlx OCA], [https://pdbe.org/5xlx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xlx RCSB], [https://www.ebi.ac.uk/pdbsum/5xlx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xlx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CHER1_PSEAE CHER1_PSEAE]] Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
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[https://www.uniprot.org/uniprot/CHER1_PSEAE CHER1_PSEAE] Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The bacterial second messenger cyclic diguanylate monophosphate (c-di-GMP) mediates multiple aspects of bacterial physiology through binding to various effectors. In some cases, these effectors are single-domain proteins which only contain a PilZ domain. It remains largely unknown how single-domain PilZ proteins function and regulate their downstream targets. Recently, a single-domain PilZ protein, MapZ (PA4608), was identified to inhibit the activity of the methyltransferase CheR1. Here, crystal structures of the C-terminal domain of CheR1 containing SAH and of CheR1 in complex with c-di-GMP-bound MapZ are reported. It was observed that the binding site of MapZ in CheR1 partially overlaps with the SAH/SAM-binding pocket. Consequently, binding of MapZ blocks SAH/SAM binding. This provides direct structural evidence on the mechanism of inhibition of CheR1 by MapZ in the presence of c-di-GMP.
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Structural basis for the regulation of chemotaxis by MapZ in the presence of c-di-GMP.,Zhu Y, Yuan Z, Gu L Acta Crystallogr D Struct Biol. 2017 Aug 1;73(Pt 8):683-691. doi:, 10.1107/S2059798317009998. Epub 2017 Jul 28. PMID:28777083<ref>PMID:28777083</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5xlx" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Protein-glutamate O-methyltransferase]]
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[[Category: Pseudomonas aeruginosa PAO1]]
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[[Category: Gu, L]]
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[[Category: Gu L]]
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[[Category: Yuan, Z]]
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[[Category: Yuan Z]]
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[[Category: Zhu, Y]]
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[[Category: Zhu Y]]
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[[Category: Methyltransferase]]
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[[Category: Signaling]]
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[[Category: Transferase]]
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Current revision

Crystal structure of the C-terminal domain of CheR1 containing SAH

PDB ID 5xlx

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