5ft8: Difference between revisions

Revision as of 07:11, 7 October 2020

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

Structural highlights

5ft8 is a 16 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	CSS, GOL, PEG, PLP
Related:	5ft4, 5ft5, 5ft6, 5ft7
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] [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.^[2] ^[3] ^[4]

References

↑ Lacourciere GM, Mihara H, Kurihara T, Esaki N, Stadtman TC. Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate. J Biol Chem. 2000 Aug 4;275(31):23769-73. PMID:10829016 doi:10.1074/jbc.M000926200
↑ Loiseau L, Ollagnier-de Choudens S, Lascoux D, Forest E, Fontecave M, Barras F. Analysis of the heteromeric CsdA-CsdE cysteine desulfurase, assisting Fe-S cluster biogenesis in Escherichia coli. J Biol Chem. 2005 Jul 22;280(29):26760-9. Epub 2005 May 18. PMID:15901727 doi:https://dx.doi.org/10.1074/jbc.M504067200
↑ Trotter V, Vinella D, Loiseau L, Ollagnier de Choudens S, Fontecave M, Barras F. The CsdA cysteine desulphurase promotes Fe/S biogenesis by recruiting Suf components and participates to a new sulphur transfer pathway by recruiting CsdL (ex-YgdL), a ubiquitin-modifying-like protein. Mol Microbiol. 2009 Dec;74(6):1527-42. PMID:20054882
↑ Miyauchi K, Kimura S, Suzuki T. A cyclic form of N6-threonylcarbamoyladenosine as a widely distributed tRNA hypermodification. Nat Chem Biol. 2013 Feb;9(2):105-11. doi: 10.1038/nchembio.1137. Epub 2012 Dec, 16. PMID:23242255 doi:https://dx.doi.org/10.1038/nchembio.1137

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OCA

[1] Lacourciere GM, Mihara H, Kurihara T, Esaki N, Stadtman TC. Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate. J Biol Chem. 2000 Aug 4;275(31):23769-73. PMID:10829016 doi:10.1074/jbc.M000926200

[2] Loiseau L, Ollagnier-de Choudens S, Lascoux D, Forest E, Fontecave M, Barras F. Analysis of the heteromeric CsdA-CsdE cysteine desulfurase, assisting Fe-S cluster biogenesis in Escherichia coli. J Biol Chem. 2005 Jul 22;280(29):26760-9. Epub 2005 May 18. PMID:15901727 doi:https://dx.doi.org/10.1074/jbc.M504067200

[3] Trotter V, Vinella D, Loiseau L, Ollagnier de Choudens S, Fontecave M, Barras F. The CsdA cysteine desulphurase promotes Fe/S biogenesis by recruiting Suf components and participates to a new sulphur transfer pathway by recruiting CsdL (ex-YgdL), a ubiquitin-modifying-like protein. Mol Microbiol. 2009 Dec;74(6):1527-42. PMID:20054882

[4] Miyauchi K, Kimura S, Suzuki T. A cyclic form of N6-threonylcarbamoyladenosine as a widely distributed tRNA hypermodification. Nat Chem Biol. 2013 Feb;9(2):105-11. doi: 10.1038/nchembio.1137. Epub 2012 Dec, 16. PMID:23242255 doi:https://dx.doi.org/10.1038/nchembio.1137

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[2]

[3]

[4]

@@ Line 1: / Line 1: @@
 ==Crystal structure of the complex between the cysteine desulfurase CsdA and the sulfur-acceptor CsdE in the persulfurated state at 2.50 Angstroem resolution==
-<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 ==
-<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FT8 FirstGlance]. <br>
+<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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/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>
+<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>
 == Function ==
@@ Line 12: / Line 12: @@
 ==See Also==
-*[[Cysteine desulfurase|Cysteine desulfurase]]
+*[[Cysteine desulfurase 3D structures|Cysteine desulfurase 3D structures]]
 *[[Selenocysteine lyase|Selenocysteine lyase]]
 == References ==
@@ Line 19: / Line 19: @@
 </StructureSection>
 [[Category: Ecoli]]
+[[Category: Large Structures]]
 [[Category: Aranda, J]]
 [[Category: Arda, A]]

5ft8: Difference between revisions

Revision as of 07:11, 7 October 2020

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

Structural highlights

Function

See Also

References

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