1r94
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(New page: 200px<br /><applet load="1r94" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r94, resolution 2.30Å" /> '''Crystal Structure of...)
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Revision as of 23:14, 20 November 2007
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Crystal Structure of IscA (MERCURY DERIVATIVE)
Overview
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.
About this Structure
1R94 is a Single protein structure of sequence from Escherichia coli with HG as ligand. Full crystallographic information is available from OCA.
Reference
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
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