6mr2: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6mr2 is ~~ON HOLD~~ ~~until Paper~~ Publication

==E. coli cysteine desulfurase SufS with a cysteine persulfide intermediate==

== Structural highlights ==

<table><tr><td colspan='2'>[[6mr2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MR2 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</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=6mr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mr2 OCA], [http://pdbe.org/6mr2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mr2 RCSB], [http://www.ebi.ac.uk/pdbsum/6mr2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mr2 ProSAT]</span></td></tr>

</table>

== Function ==

[[http://www.uniprot.org/uniprot/SUFS_ECOLI SUFS_ECOLI]] Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.<ref>PMID:10829016</ref> <ref>PMID:12089140</ref> <ref>PMID:11997471</ref> <ref>PMID:12876288</ref> <ref>PMID:12941942</ref>

== Publication Abstract from PubMed ==

SufS is a type II cysteine desulfurase and acts as the initial step in the Suf Fe-S cluster assembly pathway. In Escherichia coli this pathway is utilized under conditions of oxidative stress and is resistant to reactive oxygen species. Mechanistically this means SufS must shift between protecting a covalent persulfide intermediate and making it available for transfer to the next protein partner in the pathway, SufE. Here, we report five x-ray crystal structures of SufS including a new structure of SufS containing an inward facing persulfide intermediate on C364. Additional structures of SufS variants with substitutions at the dimer interface show changes in dimer geometry and suggest a conserved beta-hairpin structure plays a role in mediating interactions with SufE. These new structures, along with previous HDX-MS and biochemical data identify an interaction network capable of communication between active-sites of the SufS dimer coordinating the shift between desulfurase and transpersulfurase activities.

~~Authors~~:

Structural evidence for dimer-interface driven regulation of the type II cysteine desulfurase, SufS.,Dunkle JA, Bruno M, Outten FW, Frantom PA Biochemistry. 2018 Dec 20. doi: 10.1021/acs.biochem.8b01122. PMID:30571100<ref>PMID:30571100</ref>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Dunkle, J A]]

[[Category: Frantom, P A]]

[[Category: Cysteine desulfurase]]

[[Category: Persulfide]]

[[Category: Suf]]

[[Category: Transferase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6mr2 is ON HOLD  until Paper Publication
+==E. coli cysteine desulfurase SufS with a cysteine persulfide intermediate==
+<StructureSection load='6mr2' size='340' side='right' caption='[[6mr2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6mr2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MR2 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6mr6|6mr6]], [[6mre|6mre]], [[6mrh|6mrh]], [[6mri|6mri]]</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=6mr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mr2 OCA], [http://pdbe.org/6mr2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mr2 RCSB], [http://www.ebi.ac.uk/pdbsum/6mr2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mr2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/SUFS_ECOLI SUFS_ECOLI]] Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.<ref>PMID:10829016</ref> <ref>PMID:12089140</ref> <ref>PMID:11997471</ref> <ref>PMID:12876288</ref> <ref>PMID:12941942</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+SufS is a type II cysteine desulfurase and acts as the initial step in the Suf Fe-S cluster assembly pathway. In Escherichia coli this pathway is utilized under conditions of oxidative stress and is resistant to reactive oxygen species. Mechanistically this means SufS must shift between protecting a covalent persulfide intermediate and making it available for transfer to the next protein partner in the pathway, SufE. Here, we report five x-ray crystal structures of SufS including a new structure of SufS containing an inward facing persulfide intermediate on C364. Additional structures of SufS variants with substitutions at the dimer interface show changes in dimer geometry and suggest a conserved beta-hairpin structure plays a role in mediating interactions with SufE. These new structures, along with previous HDX-MS and biochemical data identify an interaction network capable of communication between active-sites of the SufS dimer coordinating the shift between desulfurase and transpersulfurase activities.
-Authors:
+Structural evidence for dimer-interface driven regulation of the type II cysteine desulfurase, SufS.,Dunkle JA, Bruno M, Outten FW, Frantom PA Biochemistry. 2018 Dec 20. doi: 10.1021/acs.biochem.8b01122. PMID:30571100<ref>PMID:30571100</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6mr2" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Dunkle, J A]]
+[[Category: Frantom, P A]]
+[[Category: Cysteine desulfurase]]
+[[Category: Persulfide]]
+[[Category: Suf]]
+[[Category: Transferase]]