5ft8: Difference between revisions

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<StructureSection load='5ft8' size='340' side='right'caption='[[5ft8]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='5ft8' size='340' side='right'caption='[[5ft8]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ft8]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FT8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FT8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ft8]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FT8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ft4|5ft4]], [[5ft5|5ft5]], [[5ft6|5ft6]], [[5ft7|5ft7]]</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=5ft8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ft8 OCA], [https://pdbe.org/5ft8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ft8 RCSB], [https://www.ebi.ac.uk/pdbsum/5ft8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ft8 ProSAT]</span></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=5ft8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ft8 OCA], [http://pdbe.org/5ft8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ft8 RCSB], [http://www.ebi.ac.uk/pdbsum/5ft8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ft8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CSDA_ECOLI CSDA_ECOLI]] Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. L-cysteine sulfinic acid is the best substrate. Functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate.<ref>PMID:10829016</ref> [[http://www.uniprot.org/uniprot/CSDE_ECOLI CSDE_ECOLI]] Stimulates the cysteine desulfurase activity of CsdA. Contains a cysteine residue (Cys-61) that acts to accept sulfur liberated via the desulfurase activity of CsdA. May be able to transfer sulfur to TcdA/CsdL. Seems to support the function of TcdA in the generation of cyclic threonylcarbamoyladenosine at position 37 (ct(6)A37) in tRNAs that read codons beginning with adenine. Does not appear to participate in Fe/S biogenesis.<ref>PMID:15901727</ref> <ref>PMID:20054882</ref> <ref>PMID:23242255</ref> 
[https://www.uniprot.org/uniprot/CSDA_ECOLI CSDA_ECOLI] Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. L-cysteine sulfinic acid is the best substrate. Functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate.<ref>PMID:10829016</ref>  


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Aranda, J]]
[[Category: Aranda J]]
[[Category: Arda, A]]
[[Category: Arda A]]
[[Category: Bruix, M]]
[[Category: Bruix M]]
[[Category: Campos-Oliva, R]]
[[Category: Campos-Oliva R]]
[[Category: Coll, M]]
[[Category: Coll M]]
[[Category: Fernandez, F J]]
[[Category: Fernandez FJ]]
[[Category: Garces, F]]
[[Category: Garces F]]
[[Category: Jimenez-Barbero, J]]
[[Category: Jimenez-Barbero J]]
[[Category: Lopez-Estepa, M]]
[[Category: Lopez-Estepa M]]
[[Category: Penya-Soler, E]]
[[Category: Penya-Soler E]]
[[Category: Round, A]]
[[Category: Round A]]
[[Category: Tunon, I]]
[[Category: Tunon I]]
[[Category: Vega, M C]]
[[Category: Vega MC]]
[[Category: L-cysteine desulfurase]]
[[Category: Sulfur acceptor]]
[[Category: Sulfur trafficking]]
[[Category: Transferase]]
[[Category: Transpersulfuration]]

Revision as of 08:24, 7 December 2022

Crystal structure of the complex between the cysteine desulfurase CsdA and the sulfur-acceptor CsdE in the persulfurated state at 2.50 Angstroem resolution

5ft8, resolution 2.50Å

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