1x0g: Difference between revisions

Revision as of 10:28, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1x0g.png

Template:STRUCTURE 1x0g

Crystal Structure of IscA with the [2Fe-2S] clusterCrystal Structure of IscA with the [2Fe-2S] cluster

Template:ABSTRACT PUBMED 16730357

About this StructureAbout this Structure

1X0G is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.

ReferenceReference

The asymmetric IscA homodimer with an exposed [2Fe-2S] cluster suggests the structural basis of the Fe-S cluster biosynthetic scaffold., Morimoto K, Yamashita E, Kondou Y, Lee SJ, Arisaka F, Tsukihara T, Nakai M, J Mol Biol. 2006 Jun 30;360(1):117-32. Epub 2006 May 15. PMID:16730357

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of IscA with the [2Fe-2S] cluster'''
+===Crystal Structure of IscA with the [2Fe-2S] cluster===
-==Overview==
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-It has been shown that the so-called scaffold proteins are vital in Fe-S cluster biosynthesis by providing an intermediate site for the assembly of Fe-S clusters. However, since no structural information on such scaffold proteins with bound Fe-S cluster intermediates is available, the structural basis of the core of Fe-S cluster biosynthesis remains poorly understood. Here we report the first Fe-S cluster-bound crystal structure of a scaffold protein, IscA, from Thermosynechococcus elongatus, which carries three strictly conserved cysteine residues. Surprisingly, one partially exposed [2Fe-2S] cluster is coordinated by two conformationally distinct IscA protomers, termed alpha and beta, with asymmetric cysteinyl ligation by Cys37, Cys101, Cys103 from alpha and Cys103 from beta. In the crystal, two alphabeta dimers form an unusual domain-swapped tetramer via central domains of beta protomers. Together with additional biochemical data supporting its physiologically relevant configuration, we propose that the unique asymmetric Fe-S cluster coordination and the resulting distinct conformational stabilities of the two IscA protomers are central to the function of IscA-type Fe-S cluster biosynthetic scaffold.
+The line below this paragraph, {{ABSTRACT_PUBMED_16730357}}, adds the Publication Abstract to the page
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 [[Category: Tetrameric]]
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