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Structural studies of tri-functional human GART
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2010 (English)In: Nucleic Acids Research, ISSN 0305-1048, E-ISSN 1362-4962, Vol. 38, no 20, 7308-19 p.Article in journal (Refereed) Published
Abstract [en]

Human purine de novo synthesis pathway contains several multi-functional enzymes, one of which, tri-functional GART, contains three enzymatic activities in a single polypeptide chain. We have solved structures of two domains bearing separate catalytic functions: glycinamide ribonucleotide synthetase and aminoimidazole ribonucleotide synthetase. Structures are compared with those of homologous enzymes from prokaryotes and analyzed in terms of the catalytic mechanism. We also report small angle X-ray scattering models for the full-length protein. These models are consistent with the enzyme forming a dimer through the middle domain. The protein has an approximate seesaw geometry where terminal enzyme units display high mobility owing to flexible linker segments. This resilient seesaw shape may facilitate internal substrate/product transfer or forwarding to other enzymes in the pathway.

Place, publisher, year, edition, pages
2010. Vol. 38, no 20, 7308-19 p.
Keyword [en]
functional enzymes, tri-functional GART
National Category
Natural Sciences
Research subject
Biophysics; Biochemistry
Identifiers
URN: urn:nbn:se:su:diva-53087DOI: 10.1093/nar/gkq595PubMedID: 20631005OAI: oai:DiVA.org:su-53087DiVA: diva2:389805
Available from: 2011-01-20 Created: 2011-01-20 Last updated: 2017-12-11Bibliographically approved

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Stenmark, Pål
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Department of Biochemistry and Biophysics
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