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6mre

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Revision as of 11:28, 1 January 2020

E. coli cysteine desulfurase SufS R92A with a cysteine persulfide intermediate

Structural highlights

6mre is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	6mr2, 6mr6, 6mrh, 6mri
Gene:	sufS, csdB, ynhB, b1680, JW1670 (ECOLI)
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]

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.

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^[6]

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

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:http://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:http://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:http://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:http://dx.doi.org/10.1074/jbc.M308004200
↑ Dunkle JA, Bruno M, Outten FW, Frantom PA. Structural evidence for dimer-interface driven regulation of the type II cysteine desulfurase, SufS. Biochemistry. 2018 Dec 20. doi: 10.1021/acs.biochem.8b01122. PMID:30571100 doi:http://dx.doi.org/10.1021/acs.biochem.8b01122

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6mre"

@@ Line 1: / Line 1: @@
 ==E. coli cysteine desulfurase SufS R92A with a cysteine persulfide intermediate==
-<StructureSection load='6mre' size='340' side='right' caption='[[6mre]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='6mre' size='340' side='right'caption='[[6mre]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[6mre]] is a 1 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=6MRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MRE FirstGlance]. <br>
@@ Line 21: / Line 21: @@
 </div>
 <div class="pdbe-citations 6mre" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cysteine desulfurase 3D structures|Cysteine desulfurase 3D structures]]
 == References ==
 <references/>
@@ Line 26: / Line 29: @@
 </StructureSection>
 [[Category: Ecoli]]
+[[Category: Large Structures]]
 [[Category: Dunkle, J A]]
 [[Category: Frantom, P A]]

6mre

From Proteopedia

Revision as of 11:28, 1 January 2020

E. coli cysteine desulfurase SufS R92A with a cysteine persulfide intermediate

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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