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PROSITE documentation PDOC51891 [for PROSITE entry PS51891]

CENP-V/GFA domain profile





Description

Centrome protein (CENP)-V is a kinetochore protein that drives the progression of mitosis by coordinating chromatin condensation, positioning of sister chromatid centromeres and targeting of the chromosome passager complex (CPC), a machinery that regulates the attachment of spindle microtubules (MTs) to kinetochores. CENP-V homologues are found in all vertebrates as well as in plants and nematodes. At the C-terminal end, CENP-V possesses an evolutionally conserved domain that comprises an array of seven cysteines and shows high structural similarity to glutathione-dependent formaldehyde-activating enzyme (Gfa), an enzyme responsible for formaldehyde detoxification in prokaryotes. CENP-V could be an enzyme that scavenges the formaldehyde produced in histone demethylation reactions. The three central cysteines and the flanking four cysteines separately coordinate to zinc, forming a catalytic center and a structural fold for a tertiary structure, respectively [1,2,3].

The main topological feature of the CENP-V/GFA domain is an extremely twisted mixed eight-stranded β-sheet (see <PDB:1X6M>. Within this β-sheet, the strands β8, β9, and β4 form a sandwich with another triple stranded mixed β-sheet (β5, β2, β1). The interconnection between the sheets is mediated by four 3(10) helices and two α helices. The sandwich arrangement of the β-strands is further buttressed by a terahedral zinc coordinated by the side chains of four cysteines. It appears that this zinc atom has only a structural role. A second zinc ion stabilizes a large hairpin loop that connects β3 and β4 via residues of three cysteines [3].

The profile we developed covers the entire CENP-V/GFA domain.

Last update:

April 2019 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

CENP_V_GFA, PS51891; CENP-V/GFA domain profile  (MATRIX)


References

1AuthorsTadeu A.M.B. Ribeiro S. Johnston J. Goldberg I. Gerloff D. Earnshaw W.C.
TitleCENP-V is required for centromere organization, chromosome alignment and cytokinesis.
SourceEMBO. J. 27:2510-2522(2008).
PubMed ID18772885
DOI10.1038/emboj.2008.175

2AuthorsHonda Z. Suzuki T. Honda H.
TitleIdentification of CENP-V as a novel microtubule-associating molecule that activates Src family kinases through SH3 domain interaction.
SourceGenes. Cells. 14:1383-1394(2009).
PubMed ID19930468
DOI10.1111/j.1365-2443.2009.01355.x

3AuthorsNeculai A.M. Neculai D. Griesinger C. Vorholt J.A. Becker S.
TitleA dynamic zinc redox switch.
SourceJ. Biol. Chem. 280:2826-2830(2005).
PubMed ID15548539
DOI10.1074/jbc.C400517200



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