Medical College of Wisconsin
CTSICores SearchResearch InformaticsREDCap

Solution structure of At3g28950 from Arabidopsis thaliana. Proteins 2008 May 01;71(2):546-51



Pubmed ID


Pubmed Central ID




Scopus ID

2-s2.0-41149118605   2 Citations


We determined the solution structure of At3g28950 from A. thaliana, a homolog of At5g39720, whose structure we solved earlier. The secondary structure of the 165-aa protein consists of a 5-strand antiparallel beta-barrel domain flanked by two alpha-helices and a 2-strand beta-sheet; an additional free C-terminal alpha-helix extends into solution. Bioinformatic searches and analyses suggest that members of this growing set of structurally related proteins have been recruited to serve a wide variety of functions ranging from gamma-glutamyl cyclotransferase activity to participation in plant responses to chemical and biotic stimuli. Expression of a human homolog is elevated in bladder cancer tissues. Expression patterns for At3g28950 and its Arabidopsis paralogs suggest that each one evolved a different physiological role. The At3g28950 structure was solved as part of a structural genomics effort, and the results demonstrate how such a project can further understanding of genome evolution in addition to sequence-structure and structure-function relationships. Proteins 2008. (c) 2008 Wiley-Liss, Inc.

Author List

de la Cruz NB, Peterson FC, Volkman BF


Francis C. Peterson PhD Professor in the Biochemistry department at Medical College of Wisconsin
Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Arabidopsis Proteins
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Secondary
jenkins-FCD Prod-444 eb4ebd1a08581aba961d3befd3b851a3c3ec6b46