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1r95
From Proteopedia
(New page: 200px<br /><applet load="1r95" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r95, resolution 2.65Å" /> '''Crystal Structure of...) |
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| - | [[Image:1r95.jpg|left|200px]]<br /><applet load="1r95" size=" | + | [[Image:1r95.jpg|left|200px]]<br /><applet load="1r95" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r95, resolution 2.65Å" /> | caption="1r95, resolution 2.65Å" /> | ||
'''Crystal Structure of IscA (native)'''<br /> | '''Crystal Structure of IscA (native)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | IscA belongs to an ancient family of proteins responsible for iron-sulfur | + | 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== | ==About this Structure== | ||
| - | 1R95 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1R95 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R95 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bilder, P | + | [[Category: Bilder, P W.]] |
[[Category: Ding, H.]] | [[Category: Ding, H.]] | ||
| - | [[Category: Newcomer, M | + | [[Category: Newcomer, M E.]] |
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: iron-sulfur cluster protein]] | [[Category: iron-sulfur cluster protein]] | ||
| Line 21: | Line 21: | ||
[[Category: tetrameric]] | [[Category: tetrameric]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:48:22 2008'' |
Revision as of 12:48, 21 February 2008
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Crystal Structure of IscA (native)
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
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 Thu Feb 21 14:48:22 2008
