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5y4r
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of a methyltransferase complex== | |
| + | <StructureSection load='5y4r' size='340' side='right' caption='[[5y4r]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5y4r]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y4R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y4R FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <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> | ||
| + | <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=5y4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y4r OCA], [http://pdbe.org/5y4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y4r RCSB], [http://www.ebi.ac.uk/pdbsum/5y4r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y4r ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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. [[http://www.uniprot.org/uniprot/CDGBP_PSEAE CDGBP_PSEAE]] Binds the second messenger bis-(3'-5') cyclic dimeric guanosine monophosphate (c-di-GMP). Can bind two c-di-GMP molecules per monomer. May play a role in bacterial second-messenger regulated processes. Binding to c-di-GMP induces a conformational change of the C- and N-termini resulting in the exposure of a highly negative surface on one side of the protein to a possible effector protein.<ref>PMID:17096419</ref> <ref>PMID:21280119</ref> <ref>PMID:21310957</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The bacterial second messenger cyclic di-GMP (c-di-GMP) has emerged as a prominent mediator of bacterial physiology, motility and pathogenicity. Cdi-GMP often regulates the function of its protein targets through a unique mechanism that involves a discrete PilZ adaptor protein. However, the molecular mechanism in c-di-GMP-mediated protein regulation is unclear. Here, we present the structure of the PilZ adaptor protein MapZ co-crystallized in complex with c-di-GMP and its protein target CheR1, a chemotaxis-regulating methyltransferase in Pseudomonas aeruginosa This co-crystal structure, together with the structure of free CheR1, revealed that the binding of c-di-GMP induces dramatic structural changes in MapZ that are crucial for CheR1 binding. Importantly, we found that restructuring and repositioning of two C-terminal helices enables MapZ to disrupt the CheR1 active site by dislodging a structural domain. The crystallographic observations are reinforced by proteinprotein binding and single cell-based flagellar motor switching analysis. Our studies further suggest that the regulation of chemotaxis by c-di-GMP through MapZ orthologs/homologs is widespread in proteobacteria, and that the use of allosterically regulated C-terminal motifs could be a common mechanism for PilZ adaptor proteins. Together, the findings provide detailed structural insights into how c-di-GMP controls the activity of an enzyme target indirectly through a PilZ adaptor protein. | ||
| - | + | Structural Analyses Unravel the Molecular Mechanism of Cyclic di-GMP Regulation of Bacterial Chemotaxis via a PilZ Adaptor Protein.,Yan XF, Xin L, Yen JT, Zeng Y, Jin S, Cheang QW, Fong RACY, Chiam KH, Liang ZX, Gao YG J Biol Chem. 2017 Nov 16. pii: M117.815704. doi: 10.1074/jbc.M117.815704. PMID:29146598<ref>PMID:29146598</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5y4r" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Protein-glutamate O-methyltransferase]] | ||
| + | [[Category: Gao, Y G]] | ||
| + | [[Category: Jin, S]] | ||
| + | [[Category: Liang, Z X]] | ||
| + | [[Category: Tan, Y J]] | ||
| + | [[Category: Xin, L]] | ||
| + | [[Category: Yan, X]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Transferase-protein binding complex]] | ||
Revision as of 06:13, 29 November 2017
Structure of a methyltransferase complex
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