7rrn: Difference between revisions

Latest revision as of 08:55, 4 June 2025

E. coli cysteine desulfurase SufS R56A

Structural highlights

7rrn is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:	CL, LLP
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4] ^[5]

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
↑ Takahashi Y, Tokumoto U. A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J Biol Chem. 2002 Aug 9;277(32):28380-3. Epub 2002 Jun 27. PMID:12089140 doi:https://dx.doi.org/10.1074/jbc.C200365200
↑ Mihara H, Kato S, Lacourciere GM, Stadtman TC, Kennedy RA, Kurihara T, Tokumoto U, Takahashi Y, Esaki N. The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H. Proc Natl Acad Sci U S A. 2002 May 14;99(10):6679-83. Epub 2002 May 7. PMID:11997471 doi:https://dx.doi.org/10.1073/pnas.102176099
↑ Loiseau L, Ollagnier-de-Choudens S, Nachin L, Fontecave M, Barras F. Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J Biol Chem. 2003 Oct 3;278(40):38352-9. Epub 2003 Jul 21. PMID:12876288 doi:https://dx.doi.org/10.1074/jbc.M305953200
↑ Outten FW, Wood MJ, Munoz FM, Storz G. The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. J Biol Chem. 2003 Nov 14;278(46):45713-9. Epub 2003 Aug 26. PMID:12941942 doi:https://dx.doi.org/10.1074/jbc.M308004200

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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] Takahashi Y, Tokumoto U. A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J Biol Chem. 2002 Aug 9;277(32):28380-3. Epub 2002 Jun 27. PMID:12089140 doi:https://dx.doi.org/10.1074/jbc.C200365200

[3] Mihara H, Kato S, Lacourciere GM, Stadtman TC, Kennedy RA, Kurihara T, Tokumoto U, Takahashi Y, Esaki N. The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H. Proc Natl Acad Sci U S A. 2002 May 14;99(10):6679-83. Epub 2002 May 7. PMID:11997471 doi:https://dx.doi.org/10.1073/pnas.102176099

[4] Loiseau L, Ollagnier-de-Choudens S, Nachin L, Fontecave M, Barras F. Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J Biol Chem. 2003 Oct 3;278(40):38352-9. Epub 2003 Jul 21. PMID:12876288 doi:https://dx.doi.org/10.1074/jbc.M305953200

[5] Outten FW, Wood MJ, Munoz FM, Storz G. The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. J Biol Chem. 2003 Nov 14;278(46):45713-9. Epub 2003 Aug 26. PMID:12941942 doi:https://dx.doi.org/10.1074/jbc.M308004200

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7rrn is ON HOLD  until sometime in the future
+==E. coli cysteine desulfurase SufS R56A==
+<StructureSection load='7rrn' size='340' side='right'caption='[[7rrn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7rrn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RRN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RRN FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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=7rrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rrn OCA], [https://pdbe.org/7rrn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rrn RCSB], [https://www.ebi.ac.uk/pdbsum/7rrn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rrn ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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>
-Authors: Dunkle, J.A., Gogar, R., Frantom, P.A.
+==See Also==
+*[[Selenocysteine lyase|Selenocysteine lyase]]
-Description: E. coli cysteine desulfurase SufS R56A
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Frantom, P.A]]
+__TOC__
-[[Category: Gogar, R]]
+</StructureSection>
-[[Category: Dunkle, J.A]]
+[[Category: Escherichia coli]]
+[[Category: Large Structures]]
+[[Category: Dunkle JA]]
+[[Category: Frantom PA]]
+[[Category: Gogar R]]

7rrn: Difference between revisions

Latest revision as of 08:55, 4 June 2025

E. coli cysteine desulfurase SufS R56A

Structural highlights

Function

See Also

References

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