1r95

<StructureSection load='1r95' size='340' side='right' caption='[[1r95]], [[Resolution|resolution]] 2.65&Aring;' scene=''>

<table><tr><td colspan='2'>[[1r95]] 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=1R95 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R95 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r94|1r94]]</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>

<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=1r95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r95 OCA], [http://pdbe.org/1r95 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r95 RCSB], [http://www.ebi.ac.uk/pdbsum/1r95 PDBsum]</span></td></tr>

[[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]

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r9/1r95_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

IscA belongs to an ancient family of proteins responsible for iron-sulfur cluster assembly in essential metabolic pathways preserved throughout evolution. We report here the 2.3 A resolution crystal structure of Escherichia coli IscA, a novel fold in which mixed beta-sheets form a compact alpha-beta sandwich domain. In contrast to the highly mobile secondary structural elements within the bacterial Fe-S scaffold protein IscU, a protein which is thought to have a similar function, the great majority of the amino acids that are conserved in IscA homologues are located in elements that constitute a well-ordered fold. However, the 10-residue C-terminal tail segment that contains two invariant cysteines critical for the Fe-S-binding function of a cyanobacterial (Synechocystis PCC) IscA homologue is not ordered in our structure. In addition, the crystal packing reveals a helical assembly that is constructed from two possible tetrameric oligomers of IscA.

Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold.,Bilder PW, Ding H, Newcomer ME Biochemistry. 2004 Jan 13;43(1):133-9. PMID:14705938<ref>PMID:14705938</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1r95" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Bilder, P W]]

[[Category: Ding, H]]

[[Category: Newcomer, M E]]

[[Category: Beta barrel]]

[[Category: Tetrameric]]