4c0r: Difference between revisions

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<StructureSection load='4c0r' size='340' side='right'caption='[[4c0r]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
<StructureSection load='4c0r' size='340' side='right'caption='[[4c0r]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4c0r]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25175 Atcc 25175]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C0R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C0R FirstGlance]. <br>
<table><tr><td colspan='2'>[[4c0r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C0R FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDS:OXIDIZED+GLUTATHIONE+DISULFIDE'>GDS</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GDS:OXIDIZED+GLUTATHIONE+DISULFIDE'>GDS</scene></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=4c0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0r OCA], [http://pdbe.org/4c0r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c0r RCSB], [http://www.ebi.ac.uk/pdbsum/4c0r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0r 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=4c0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0r OCA], [https://pdbe.org/4c0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c0r RCSB], [https://www.ebi.ac.uk/pdbsum/4c0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0r ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[[https://www.uniprot.org/uniprot/Q93DA5_STRMG Q93DA5_STRMG]]
Glutathione (GSH) protects cells against oxidative injury and maintains a range of vital functions across all branches of life. Despite recent advances in our understanding of the transport mechanisms responsible for maintaining the spatiotemporal homeostasis of GSH and its conjugates in eukaryotes and Gram-negative bacteria, the molecular and structural basis of GSH import into Gram-positive bacteria has remained largely uncharacterized. Here, we employ genetic, biochemical and structural studies to investigate a possible glutathione import axis in Streptococcus mutans, an organism that has hitherto served as a model system. We show that GshT, a type 3 solute binding protein, displays physiologically relevant affinity for GSH and glutathione disulfide (GSSG). The crystal structure of GshT in complex with GSSG reveals a collapsed structure whereby the GS-I-leg of GSSG is accommodated tightly via extensive interactions contributed by the N- and C-terminal lobes of GshT, while the GS-II leg extends to the solvent. This can explain the ligand promiscuity of GshT in terms of binding glutathione analogues with substitutions at the cysteine-sulfur or the glycine-carboxylate. Finally, we show that GshT primes glutathione import via the l-cystine ABC transporter TcyBC, a membrane permease, which had previously exclusively been associated with the transport of l-cystine.
 
Molecular and structural basis of glutathione import in Gram-positive bacteria via GshT and the cystine ABC importer TcyBC of Streptococcus mutans.,Vergauwen B, Verstraete K, Senadheera DB, Dansercoer A, Cvitkovitch DG, Guedon E, Savvides SN Mol Microbiol. 2013 Jul;89(2):288-303. doi: 10.1111/mmi.12274. Epub 2013 Jun 10. PMID:23701283<ref>PMID:23701283</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4c0r" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 25175]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cvitkovitch, D G]]
[[Category: Streptococcus mutans]]
[[Category: Dansercoer, A]]
[[Category: Cvitkovitch DG]]
[[Category: Guedon, E]]
[[Category: Dansercoer A]]
[[Category: Savvides, S N]]
[[Category: Guedon E]]
[[Category: Senadheera, D B]]
[[Category: Savvides SN]]
[[Category: Vergauwen, B]]
[[Category: Senadheera DB]]
[[Category: Verstraete, K]]
[[Category: Vergauwen B]]
[[Category: Transport protein]]
[[Category: Verstraete K]]

Revision as of 17:19, 7 September 2022

Molecular and structural basis of glutathione import in Gram-positive bacteria via GshT and the cystine ABC importer TcyBC of Streptococcus mutans.

4c0r, resolution 1.55Å

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