2qd0: Difference between revisions
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'''Crystal structure of mitoNEET''' | {{Structure | ||
|PDB= 2qd0 |SIZE=350|CAPTION= <scene name='initialview01'>2qd0</scene>, resolution 1.810Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FES:FE2/S2 (INORGANIC) CLUSTER'>FES</scene> | |||
|ACTIVITY= | |||
|GENE= ZCD1, C10orf70 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Crystal structure of mitoNEET''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2QD0 is a [ | 2QD0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QD0 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of human mitoNEET reveals distinct groups of iron sulfur proteins., Lin J, Zhou T, Ye K, Wang J, Proc Natl Acad Sci U S A. 2007 Sep 11;104(37):14640-5. Epub 2007 Aug 31. PMID:[http:// | Crystal structure of human mitoNEET reveals distinct groups of iron sulfur proteins., Lin J, Zhou T, Ye K, Wang J, Proc Natl Acad Sci U S A. 2007 Sep 11;104(37):14640-5. Epub 2007 Aug 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17766439 17766439] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: metal binding protein]] | [[Category: metal binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:24:32 2008'' | ||
Revision as of 19:24, 20 March 2008
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| , resolution 1.810Å | |||||||
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| Ligands: | |||||||
| Gene: | ZCD1, C10orf70 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of mitoNEET
OverviewOverview
MitoNEET is a protein of unknown function present in the mitochondrial membrane that was recently shown to bind specifically the antidiabetic drug pioglizatone. Here, we report the crystal structure of the soluble domain (residues 32-108) of human mitoNEET at 1.8-A resolution. The structure reveals an intertwined homodimer, and each subunit was observed to bind a [2Fe-2S] cluster. The [2Fe-2S] ligation pattern of three cysteines and one histidine differs from the known pattern of four cysteines in most cases or two cysteines and two histidines as observed in Rieske proteins. The [2Fe-2S] cluster is packed in a modular structure formed by 17 consecutive residues. The cluster-binding motif is conserved in at least seven distinct groups of proteins from bacteria, archaea, and eukaryotes, which show a consensus sequence of (hb)-C-X(1)-C-X(2)-(S/T)-X(3)-P-(hb)-C-D-X(2)-H, where hb represents a hydrophobic residue; we term this a CCCH-type [2Fe-2S] binding motif. The nine conserved residues in the motif contribute to iron ligation and structure stabilization. UV-visible absorption spectra indicated that mitoNEET can exist in oxidized and reduced states. Our study suggests an electron transfer function for mitoNEET and for other proteins containing the CCCH motif.
About this StructureAbout this Structure
2QD0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human mitoNEET reveals distinct groups of iron sulfur proteins., Lin J, Zhou T, Ye K, Wang J, Proc Natl Acad Sci U S A. 2007 Sep 11;104(37):14640-5. Epub 2007 Aug 31. PMID:17766439 [[Category: [2fe-2s]]]
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