Crystal structure of YegS, a homologue to the mammalian diacylglycerol kinases, reveals a novel regulatory metal binding site

Bakali, Amin (author): Stockholms universitet,Institutionen för biokemi och biofysik

Herman, Maria Dolores (author)

Johnson, Kenneth A. (author)

Kelly, Amélie A. (author)

Wieslander, Åke (author): Stockholms universitet,Institutionen för biokemi och biofysik

(creator_code:org_t)

2007
2007
English.
In: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 282:27, s. 19644-19652

Related links:: https://urn.kb.se/re...; show more...; https://doi.org/10.1...; http://kipublication...; show less...

Abstract Subject headings

The human lipid kinase family controls cell proliferation, differentiation, and tumorigenesis and includes diacylglycerol kinases, sphingosine kinases, and ceramide kinases. YegS is an Escherichia coli protein with significant sequence homology to the catalytic domain of the human lipid kinases. We have solved the crystal structure of YegS and shown that it is a lipid kinase with phosphatidylglycerol kinase activity. The crystal structure reveals a two-domain protein with significant structural similarity to a family of NAD kinases. The active site is located in the interdomain cleft formed by four conserved sequence motifs. Surprisingly, the structure reveals a novel metal binding site composed of residues conserved in most lipid kinases.

By the author/editor: Bakali, Amin; Herman, Maria Do ...; Johnson, Kenneth ...; Kelly, Amélie A.; Wieslander, Åke; Hallberg, B. M.; show more...; Nordlund, Pär; show less...

About the subject

MEDICAL AND HEALTH SCIENCES: MEDICAL AND HEAL ...; and Medical Biotechn ...; and Medical Biotechn ...

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