4lw4: Difference between revisions

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<StructureSection load='4lw4' size='340' side='right'caption='[[4lw4]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
<StructureSection load='4lw4' size='340' side='right'caption='[[4lw4]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4lw4]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LW4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4lw4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_IHE3034 Escherichia coli IHE3034] and [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=4LW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LW4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 2.01&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4lw2|4lw2]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=4lw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lw4 OCA], [https://pdbe.org/4lw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lw4 RCSB], [https://www.ebi.ac.uk/pdbsum/4lw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lw4 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=4lw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lw4 OCA], [https://pdbe.org/4lw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lw4 RCSB], [https://www.ebi.ac.uk/pdbsum/4lw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lw4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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>
[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>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli IHE3034]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kim, S]]
[[Category: Kim S]]
[[Category: Park, S Y]]
[[Category: Park SY]]
[[Category: Csda]]
[[Category: Cysteine desulfurase]]
[[Category: Lyase]]
[[Category: Sufe]]

Latest revision as of 14:38, 8 November 2023

Structural changes during cysteine desulfurase CsdA and sulfur-acceptor CsdE interactions provide insight into the trans-persulfuration

4lw4, resolution 2.01Å

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