This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5xlx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:19, 27 March 2024) (edit) (undo)
 
Line 3: Line 3:
<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 ==
-
<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>
+
<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>
-
</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>
+
</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>
-
<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='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>
-
<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>
+
<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 ==
-
[[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.
+
[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.
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
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.
+
-
 
+
-
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>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5xlx" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Protein-glutamate O-methyltransferase]]
+
[[Category: Pseudomonas aeruginosa PAO1]]
-
[[Category: Gu, L]]
+
[[Category: Gu L]]
-
[[Category: Yuan, Z]]
+
[[Category: Yuan Z]]
-
[[Category: Zhu, Y]]
+
[[Category: Zhu Y]]
-
[[Category: Methyltransferase]]
+
-
[[Category: Signaling]]
+
-
[[Category: Transferase]]
+

Current revision

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

PDB ID 5xlx

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5xlx"
Personal tools