Change search
ReferencesLink to record
Permanent link

Direct link
Structural studies of tri-functional human GART
Show others and affiliations
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
URN: urn:nbn:se:su:diva-53087DOI: 10.1093/nar/gkq595PubMedID: 20631005OAI: diva2:389805
Available from: 2011-01-20 Created: 2011-01-20 Last updated: 2011-02-16Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Stenmark, Pål
By organisation
Department of Biochemistry and Biophysics
In the same journal
Nucleic Acids Research
Natural Sciences

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 31 hits
ReferencesLink to record
Permanent link

Direct link