5y4s: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5y4s is ~~ON HOLD until Paper~~ Publication

==Structure of a methyltransferase complex==

== Structural highlights ==

<table><tr><td colspan='2'>[[5y4s]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y4S FirstGlance]. <br>

</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=5y4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y4s OCA], [http://pdbe.org/5y4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y4s RCSB], [http://www.ebi.ac.uk/pdbsum/5y4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y4s 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.

== 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.

~~Authors:~~ Yan~~, X.~~, Xin, L., ~~Tan~~, Y~~.J.~~, Jin, S., Liang, Z.X.~~, Gao, Y~~.G.

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>

~~Description: Structure~~ of ~~a methyltransferase complex~~

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

~~[[Category~~: ~~Unreleased Structures]]~~

</div>

[[Category: ~~Liang, Z.X~~]]

[[Category: Gao, Y.G]]

== 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: ~~Tan, Y.J]]~~

[[Category: Transferase]]

~~[[Category: Xin, L~~]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5y4s is ON HOLD  until Paper Publication
+==Structure of a methyltransferase complex==
+<StructureSection load='5y4s' size='340' side='right' caption='[[5y4s]], [[Resolution|resolution]] 3.41&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5y4s]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y4S FirstGlance]. <br>
+</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=5y4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y4s OCA], [http://pdbe.org/5y4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y4s RCSB], [http://www.ebi.ac.uk/pdbsum/5y4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y4s 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.
+<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.
-Authors: Yan, X., Xin, L., Tan, Y.J., Jin, S., Liang, Z.X., Gao, Y.G.
+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>
-Description: Structure of a methyltransferase complex
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Liang, Z.X]]
+<div class="pdbe-citations 5y4s" style="background-color:#fffaf0;"></div>
-[[Category: Gao, Y.G]]
+== 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: Tan, Y.J]]
+[[Category: Transferase]]
-[[Category: Xin, L]]