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1r95
From Proteopedia
Revision as of 16:18, 29 September 2014 by OCA (Talk | contribs)
1r95 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Bilder PW, Ding H, Newcomer ME. Crystal structure of the ancient, Fe-S scaffold IscA reveals a novel protein fold. Biochemistry. 2004 Jan 13;43(1):133-9. PMID:14705938 doi:10.1021/bi035440s
