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Crystal structure o...
Crystal structure of YegS, a homologue to the mammalian diacylglycerol kinases, reveals a novel regulatory metal binding site
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- Bakali, Amin (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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Herman, Maria Dolores (author)
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Johnson, Kenneth A. (author)
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Kelly, Amélie A. (author)
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- Wieslander, Åke (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Hallberg, B. M. (author)
- Karolinska Institutet
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- Nordlund, Pär (author)
- Karolinska Institutet
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(creator_code:org_t)
- 2007
- 2007
- English.
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In: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 282:27, s. 19644-19652
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- 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.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinsk bioteknologi -- Medicinsk bioteknologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Medical Biotechnology -- Medical Biotechnology (hsv//eng)
Keyword
- Biochemistry
- Biokemi
Publication and Content Type
- ref (subject category)
- art (subject category)
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