1r94
From Proteopedia
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|PDB= 1r94 |SIZE=350|CAPTION= <scene name='initialview01'>1r94</scene>, resolution 2.30Å | |PDB= 1r94 |SIZE=350|CAPTION= <scene name='initialview01'>1r94</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene> | + | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= YFHF, B2528, C3053, Z3795, ECS3394, SF2575, S2747 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= YFHF, B2528, C3053, Z3795, ECS3394, SF2575, S2747 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1r95|1R95]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r94 OCA], [http://www.ebi.ac.uk/pdbsum/1r94 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r94 RCSB]</span> | ||
}} | }} | ||
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[[Category: Ding, H.]] | [[Category: Ding, H.]] | ||
[[Category: Newcomer, M E.]] | [[Category: Newcomer, M E.]] | ||
| - | [[Category: HG]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: iron-sulfur cluster protein]] | [[Category: iron-sulfur cluster protein]] | ||
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[[Category: tetrameric]] | [[Category: tetrameric]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:24:52 2008'' |
Revision as of 20:24, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | YFHF, B2528, C3053, Z3795, ECS3394, SF2575, S2747 (Escherichia coli) | ||||||
| Related: | 1R95
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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