5awf: Difference between revisions

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<StructureSection load='5awf' size='340' side='right'caption='[[5awf]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
<StructureSection load='5awf' size='340' side='right'caption='[[5awf]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5awf]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AWF FirstGlance]. <br>
<table><tr><td colspan='2'>[[5awf]] is a 8 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=5AWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AWF FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5awg|5awg]]</div></td></tr>
</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=5awf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awf OCA], [https://pdbe.org/5awf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5awf RCSB], [https://www.ebi.ac.uk/pdbsum/5awf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5awf ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sufB, ynhE, b1683, JW5273 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), sufD, ynhC, b1681, JW1671 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), sufC, ynhD, b1682, JW1672 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=5awf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awf OCA], [https://pdbe.org/5awf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5awf RCSB], [https://www.ebi.ac.uk/pdbsum/5awf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5awf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SUFB_ECOLI SUFB_ECOLI]] The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.<ref>PMID:12941942</ref>  [[https://www.uniprot.org/uniprot/SUFC_ECOLI SUFC_ECOLI]] Has low ATPase activity. The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.<ref>PMID:12554644</ref> <ref>PMID:12941942</ref>  [[https://www.uniprot.org/uniprot/SUFD_ECOLI SUFD_ECOLI]] The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the FhuF protein.<ref>PMID:10322040</ref> <ref>PMID:12941942</ref>
[https://www.uniprot.org/uniprot/SUFB_ECOLI SUFB_ECOLI] The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation.<ref>PMID:12941942</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: Ecoli]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Hirabayashi, K]]
[[Category: Hirabayashi K]]
[[Category: Wada, K]]
[[Category: Wada K]]
[[Category: Abc atpase]]
[[Category: Abc protein]]
[[Category: Iron-sulfur cluster]]
[[Category: Iron-sulfur protein]]
[[Category: Transport protein-protein binding complex]]

Revision as of 06:27, 31 May 2023

Crystal structure of SufB-SufC-SufD complex from Escherichia coli

5awf, resolution 2.96Å

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