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.


7qoe

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:53, 1 May 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='7qoe' size='340' side='right'caption='[[7qoe]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
<StructureSection load='7qoe' size='340' side='right'caption='[[7qoe]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[7qoe]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QOE FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[7qoe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptospira_levettii Leptospira levettii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QOE FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 1.2&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=7qoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qoe OCA], [https://pdbe.org/7qoe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qoe RCSB], [https://www.ebi.ac.uk/pdbsum/7qoe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qoe 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=7qoe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qoe OCA], [https://pdbe.org/7qoe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qoe RCSB], [https://www.ebi.ac.uk/pdbsum/7qoe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qoe ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/A0A2N0AXP5_9LEPT A0A2N0AXP5_9LEPT]
-
The bacterial stringent response involves wide-ranging metabolic reprogramming aimed at increasing long-term survivability during stress conditions. One of the hallmarks of the stringent response is the production of a set of modified nucleotides, known as alarmones, which affect a multitude of cellular pathways in diverse ways. Production and degradation of these molecules depend on the activity of enzymes from the RelA/SpoT homologous (RSH) family, which come in both bifunctional (containing domains to both synthesize and hydrolyze alarmones) and monofunctional (consisting of only synthetase or hydrolase domain) variants, of which the structure, activity, and regulation of the bifunctional RSHs have been studied most intensely. Despite playing an important role in guanosine nucleotide homeostasis in particular, mechanisms of regulation of the small alarmone hydrolases (SAH) are still rather unclear. Here, we present crystal structures of SAH enzymes from Corynebacterium glutamicum (RelHCg) and Leptospira levettii (RelHLl) and show that while being highly similar, structural differences in substrate access and dimer conformations might be important for regulating their activity. We propose that a varied dimer form is a general property of the SAH family, based on current structural information as well as prediction models for this class of enzymes. Finally, subtle structural variations between monofunctional and bifunctional enzymes point to how these different classes of enzymes are regulated.
+
-
 
+
-
Structural variations between small alarmone hydrolase dimers support different modes of regulation of the stringent response.,Bisiak F, Chrenkova A, Zhang SD, Pedersen JN, Otzen DE, Zhang YE, Brodersen DE J Biol Chem. 2022 Jun 14:102142. doi: 10.1016/j.jbc.2022.102142. PMID:35714769<ref>PMID:35714769</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 7qoe" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Bisiak, F]]
+
[[Category: Leptospira levettii]]
-
[[Category: Brodersen, D E]]
+
[[Category: Bisiak F]]
-
[[Category: Chrenkova, A]]
+
[[Category: Brodersen DE]]
-
[[Category: Alarmone]]
+
[[Category: Chrenkova A]]
-
[[Category: Hd domain]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Stress response]]
+

Current revision

Structure of a small alarmone hydrolase from Leptospira levettii

PDB ID 7qoe

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/7qoe"
Personal tools