1r95

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{{STRUCTURE_1r95| PDB=1r95 | SCENE= }}
{{STRUCTURE_1r95| PDB=1r95 | SCENE= }}
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'''Crystal Structure of IscA (native)'''
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===Crystal Structure of IscA (native)===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_14705938}}
==About this Structure==
==About this Structure==
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[[Category: Pseudo-asymmetric motif]]
[[Category: Pseudo-asymmetric motif]]
[[Category: Tetrameric]]
[[Category: Tetrameric]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:14:19 2008''

Revision as of 08:14, 28 July 2008

Image:1r95.png

Template:STRUCTURE 1r95

Crystal Structure of IscA (native)

Template:ABSTRACT PUBMED 14705938

About this Structure

1R95 is a Single protein structure of sequence from Escherichia coli. 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

Page seeded by OCA on Mon Jul 28 11:14:19 2008

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