6uy5: Difference between revisions

Line 1:

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

~~The entry~~ 6uy5 is ~~ON HOLD~~ ~~until Paper Publication~~

==E. coli cysteine desulfurase SufS with a spontaneously rotated beta-hairpin==

~~Authors~~:

== Structural highlights ==

<table><tr><td colspan='2'>[[6uy5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UY5 OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6UY5 FirstGlance].

~~Description~~:

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

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

<tr id='NonStdRes'><td class="sblockLbl">[[Non-Standard_Residue|NonStd Res:]]</td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene></td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6uy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uy5 OCA], [http://pdbe.org/6uy5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uy5 RCSB], [http://www.ebi.ac.uk/pdbsum/6uy5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uy5 ProSAT]</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>

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Dunkle, J A]]

[[Category: Frantom, P A]]

[[Category: Cysteine desulfurase]]

[[Category: Lyase]]

[[Category: Persulfide]]

[[Category: Plp]]

[[Category: Suf]]

[[Category: Transferase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6uy5 is ON HOLD  until Paper Publication
+==E. coli cysteine desulfurase SufS with a spontaneously rotated beta-hairpin==
+<StructureSection load='6uy5' size='340' side='right'caption='[[6uy5]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6uy5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UY5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6UY5 FirstGlance]. <br>
-Description:
+</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>
-[[Category: Unreleased Structures]]
+<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=6uy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uy5 OCA], [http://pdbe.org/6uy5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uy5 RCSB], [http://www.ebi.ac.uk/pdbsum/6uy5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uy5 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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Dunkle, J A]]
+[[Category: Frantom, P A]]
+[[Category: Cysteine desulfurase]]
+[[Category: Lyase]]
+[[Category: Persulfide]]
+[[Category: Plp]]
+[[Category: Suf]]
+[[Category: Transferase]]