2JQV

Solution structure At3g28950.1 from Arabidopsis thaliana

Summary for 2JQV

• Entry DOI: 10.2210/pdb2jqv/pdb
• NMR Information: BMRB: 15295
• Descriptor: AIG2 protein-like (1 entity in total)
• Functional Keywords: at3g28950.1, structural genomics, protein structure initiative, psi, center for eukaryotic structural genomics, cesg
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 1
• Total formula weight: 18596.74

Authors

Volkman, B.F.,de la Cruz, N.B.,Peterson, F.C.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2007-06-07, release date: 2007-08-14, Last modification date: 2023-12-20)

Primary citation

de la Cruz, N.B.,Peterson, F.C.,Volkman, B.F.
Solution structure of At3g28950 from Arabidopsis thaliana.
Proteins, 71:546-551, 2008

PubMed Abstract: 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.

PubMed: 18214976
DOI: 10.1002/prot.21936

Experimental method

SOLUTION NMR