3fm0

Crystal structure of WD40 protein Ciao1Crystal structure of WD40 protein Ciao1

Structural highlights

3fm0 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.7Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CIAO1_HUMAN Key component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. Seems to specifically modulate the transactivation activity of WT1. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The WD40 domain exhibits a beta-propeller architecture, often comprising seven blades. The WD40 domain is one of the most abundant domains and also among the top interacting domains in eukaryotic genomes. In this review, we will discuss the identification, definition and architecture of the WD40 domains. WD40 domain proteins are involved in a large variety of cellular processes, in which WD40 domains function as a protein-protein or protein-DNA interaction platform. WD40 domain mediates molecular recognition events mainly through the smaller top surface, but also through the bottom surface and sides. So far, no WD40 domain has been found to display enzymatic activity. We will also discuss the different binding modes exhibited by the large versatile family of WD40 domain proteins. In the last part of this review, we will discuss how post-translational modifications are recognized by WD40 domain proteins.

Structure and function of WD40 domain proteins.,Xu C, Min J Protein Cell. 2011 Mar;2(3):202-14. Epub 2011 Apr 6. PMID:21468892^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Srinivasan V, Netz DJ, Webert H, Mascarenhas J, Pierik AJ, Michel H, Lill R. Structure of the yeast WD40 domain protein Cia1, a component acting late in iron-sulfur protein biogenesis. Structure. 2007 Oct;15(10):1246-57. PMID:17937914 doi:10.1016/j.str.2007.08.009
↑ Ito S, Tan LJ, Andoh D, Narita T, Seki M, Hirano Y, Narita K, Kuraoka I, Hiraoka Y, Tanaka K. MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in chromosome segregation. Mol Cell. 2010 Aug 27;39(4):632-40. doi: 10.1016/j.molcel.2010.07.029. PMID:20797633 doi:http://dx.doi.org/10.1016/j.molcel.2010.07.029
↑ Xu C, Min J. Structure and function of WD40 domain proteins. Protein Cell. 2011 Mar;2(3):202-14. Epub 2011 Apr 6. PMID:21468892 doi:10.1007/s13238-011-1018-1

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OCA

[1] Srinivasan V, Netz DJ, Webert H, Mascarenhas J, Pierik AJ, Michel H, Lill R. Structure of the yeast WD40 domain protein Cia1, a component acting late in iron-sulfur protein biogenesis. Structure. 2007 Oct;15(10):1246-57. PMID:17937914 doi:10.1016/j.str.2007.08.009

[2] Ito S, Tan LJ, Andoh D, Narita T, Seki M, Hirano Y, Narita K, Kuraoka I, Hiraoka Y, Tanaka K. MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in chromosome segregation. Mol Cell. 2010 Aug 27;39(4):632-40. doi: 10.1016/j.molcel.2010.07.029. PMID:20797633 doi:http://dx.doi.org/10.1016/j.molcel.2010.07.029

[3] Xu C, Min J. Structure and function of WD40 domain proteins. Protein Cell. 2011 Mar;2(3):202-14. Epub 2011 Apr 6. PMID:21468892 doi:10.1007/s13238-011-1018-1

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