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1s98

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Revision as of 15:31, 27 October 2021

E.coli IscA crystal structure to 2.3 A

Structural highlights

1s98 is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	YFHF, B2528, C3053, Z3795, ECS3394, SF2575, S2747 ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ISCA_ECOLI] Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system TrxA/TrxB.[HAMAP-Rule:MF_01429]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

IscA, an 11 kDa member of the hesB family of proteins, binds iron and [2Fe-2S] clusters, and participates in the biosynthesis of iron-sulfur proteins. We report the crystal structure of the apo-protein form of IscA from Escherichia coli to a resolution of 2.3A. The crystals belong to the space group P3(2)21 and have unit cell dimensions a=b=66.104 A, c=150.167 A (alpha=beta=90 degrees, gamma=120 degrees ). The structure was solved using single-wavelength anomalous dispersion (SAD) phasing of a selenomethionyl derivative, and the IscA model was refined to R=21.4% (Rfree=25.4%). IscA exists as an (alpha1alpha2)2 homotetramer with the (alpha1alpha2) dimer comprising the asymmetric unit. Cys35, implicated in Fe-S cluster assembly, is located in a central cavity formed at the tetramer interface with the gamma-sulfur atoms of residues from the alpha1 and alpha2' monomers (and alpha1'alpha2) positioned close to one another (approximately equal 7 A). C-terminal residues 99-107 are disordered, and the exact positions of Cys99 and Cys101 could not be determined. However, computer modeling of C-terminal residues in the tetramer suggests that Cys99 and Cys101 in the alpha1 monomer and those of the alpha1' monomer (or alpha2 and alpha2') are positioned sufficiently close to coordinate [2Fe-2S] clusters between the two dimers, whereas this is not possible within the (alpha1alpha2) or (alpha1'alpha2') dimer. This symmetrical arrangement allows for binding of two [2Fe-2S] clusters on opposite sides of the tetramer. Modeling further reveals that Cys101 is positioned sufficiently close to Cys35 to allow Cys35 to participate in cluster assembly, formation, or transfer.

Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli.,Cupp-Vickery JR, Silberg JJ, Ta DT, Vickery LE J Mol Biol. 2004 Apr 16;338(1):127-37. PMID:15050828^[1]

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

References

↑ Cupp-Vickery JR, Silberg JJ, Ta DT, Vickery LE. Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli. J Mol Biol. 2004 Apr 16;338(1):127-37. PMID:15050828 doi:10.1016/j.jmb.2004.02.027

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1s98"

@@ Line 3: / Line 3: @@
 <StructureSection load='1s98' size='340' side='right'caption='[[1s98]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1s98]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S98 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1S98 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1s98]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S98 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YFHF, B2528, C3053, Z3795, ECS3394, SF2575, S2747 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YFHF, B2528, C3053, Z3795, ECS3394, SF2575, S2747 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1s98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s98 OCA], [http://pdbe.org/1s98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s98 RCSB], [http://www.ebi.ac.uk/pdbsum/1s98 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s98 ProSAT]</span></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=1s98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s98 OCA], [https://pdbe.org/1s98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s98 RCSB], [https://www.ebi.ac.uk/pdbsum/1s98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s98 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ISCA_ECOLI ISCA_ECOLI]] Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system TrxA/TrxB.[HAMAP-Rule:MF_01429]
+[[https://www.uniprot.org/uniprot/ISCA_ECOLI ISCA_ECOLI]] Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system TrxA/TrxB.[HAMAP-Rule:MF_01429]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1s98

From Proteopedia

Revision as of 15:31, 27 October 2021

E.coli IscA crystal structure to 2.3 A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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