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.


5kav

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:05, 1 March 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==The structure of SAV2435==
==The structure of SAV2435==
-
<StructureSection load='5kav' size='340' side='right' caption='[[5kav]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+
<StructureSection load='5kav' size='340' side='right'caption='[[5kav]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5kav]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KAV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KAV FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5kav]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_N315 Staphylococcus aureus subsp. aureus N315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KAV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KAV FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2&#8491;</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=5kav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kav OCA], [http://pdbe.org/5kav PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kav RCSB], [http://www.ebi.ac.uk/pdbsum/5kav PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kav ProSAT]</span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5kav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kav OCA], [https://pdbe.org/5kav PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kav RCSB], [https://www.ebi.ac.uk/pdbsum/5kav PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kav ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/A0A0H3JRN6_STAAN A0A0H3JRN6_STAAN]
-
Multidrug resistance (MDR) refers to the acquired ability of cells to tolerate a broad range of toxic compounds. One mechanism cells employ is to increase the level of expression of efflux pumps for the expulsion of xenobiotics. A key feature uniting efflux-related mechanisms is multidrug (MD) recognition, either by efflux pumps themselves or by their transcriptional regulators. However, models describing MD binding by MDR effectors are incomplete, underscoring the importance of studies focused on the recognition elements and key motifs that dictate polyspecific binding. One such motif is the GyrI-like domain, which is found in several MDR proteins and is postulated to have been adapted for small-molecule binding and signaling. Here we report the solution binding properties and crystal structures of two proteins containing GyrI-like domains, SAV2435 and CTR107, bound to various ligands. Furthermore, we provide a comparison with deposited crystal structures of GyrI-like proteins, revealing key features of GyrI-like domains that not only support polyspecific binding but also are conserved among GyrI-like domains. Together, our studies suggest that GyrI-like domains perform evolutionarily conserved functions connected to multidrug binding and highlight the utility of these types of studies for elucidating mechanisms of MDR.
+
-
 
+
-
Solution Binding and Structural Analyses Reveal Potential Multidrug Resistance Functions for SAV2435 and CTR107 and Other GyrI-like Proteins.,Moreno A, Froehlig JR, Bachas S, Gunio D, Alexander T, Vanya A, Wade H Biochemistry. 2016 Aug 30;55(34):4850-63. doi: 10.1021/acs.biochem.6b00651. Epub , 2016 Aug 18. PMID:27505298<ref>PMID:27505298</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5kav" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Moreno, A]]
+
[[Category: Large Structures]]
-
[[Category: Wade, H]]
+
[[Category: Staphylococcus aureus subsp. aureus N315]]
-
[[Category: Gyri-like domatin]]
+
[[Category: Moreno A]]
-
[[Category: Multi-drug recognition]]
+
[[Category: Wade H]]
-
[[Category: Unknown function]]
+

Current revision

The structure of SAV2435

PDB ID 5kav

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/5kav"
Personal tools