8ips: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8ips]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IPS FirstGlance]. <br>
<table><tr><td colspan='2'>[[8ips]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IPS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=8ips FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ips OCA], [https://pdbe.org/8ips PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ips RCSB], [https://www.ebi.ac.uk/pdbsum/8ips PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ips 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=8ips FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ips OCA], [https://pdbe.org/8ips PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ips RCSB], [https://www.ebi.ac.uk/pdbsum/8ips PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ips ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/A0A140NDD5_ECOBD A0A140NDD5_ECOBD]  
[https://www.uniprot.org/uniprot/CYDC_ECOLI CYDC_ECOLI] Part of the ABC transporter complex CydDC that exports the reduced low-molecular-weight thiols cysteine and glutathione to the periplasm (PubMed:12393891, PubMed:16040611). Export of these thiol-containing redox-active molecules may be crucial for redox homeostasis in the periplasm, permitting correct assembly of various respiratory complexes and formation of correct disulfide bonds in periplasmic and secreted proteins (Probable). CydC contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation (PubMed:24958725). Required for the assembly of functional cytochrome bd-type quinol oxidases and periplasmic c-type cytochromes (PubMed:15470119, PubMed:3032907, PubMed:7934832, PubMed:8181727). Overexpression of CydDC under anaerobic conditions also results in the formation of a heme biosynthesis-derived pigment, P-574 (PubMed:12375104). CydDC binds heme b, but heme is probably not transported by the complex and instead has a role in regulating ATPase activity (PubMed:24958725).<ref>PMID:12375104</ref> <ref>PMID:12393891</ref> <ref>PMID:15470119</ref> <ref>PMID:16040611</ref> <ref>PMID:24958725</ref> <ref>PMID:3032907</ref> <ref>PMID:7934832</ref> <ref>PMID:8181727</ref> <ref>PMID:12393891</ref> <ref>PMID:16040611</ref> <ref>PMID:31279084</ref>  Conversely, a more recent study suggests an alternative function of CydDC: authors suggest that CydDC does not mediate the export of L-cysteine but rather reduces cytoplasmic L-cystine to L-cysteine (PubMed:32900959). The principle function of CydDC would be to maintain the reduced state of cytoplasmic L-cysteine, thereby providing an important connection between sulfur metabolism, oxidative stress and resistance to antibiotics (PubMed:32900959).<ref>PMID:32900959</ref>
== References ==
<references/>
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</StructureSection>
</StructureSection>
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