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Solution structure of Arabidopsis thaliana protein At5g39720.1, a member of the AIG2-like protein family. Acta Crystallogr Sect F Struct Biol Cryst Commun 2006 Jun 01;62(Pt 6):490-3

Date

06/07/2006

Pubmed ID

16754964

Pubmed Central ID

PMC2243094

DOI

10.1107/S1744309106015946

Scopus ID

2-s2.0-33745138479   6 Citations

Abstract

The three-dimensional structure of Arabidopsis thaliana protein At5g39720.1 was determined by NMR spectroscopy. It is the first representative structure of Pfam family PF06094, which contains protein sequences similar to that of AIG2, an A. thaliana protein of unknown function induced upon infection by the bacterial pathogen Pseudomonas syringae. The At5g39720.1 structure consists of a five-stranded beta-barrel surrounded by two alpha-helices and a small beta-sheet. A long flexible alpha-helix protrudes from the structure at the C-terminal end. A structural homology search revealed similarity to three members of Pfam family UPF0131. Conservation of residues in a hydrophilic cavity able to bind small ligands in UPF0131 proteins suggests that this may also serve as an active site in AIG2-like proteins.

Author List

Lytle BL, Peterson FC, Tyler EM, Newman CL, Vinarov DA, Markley JL, Volkman BF

Authors

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
Binding Sites
Conserved Sequence
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
Protein Structure, Secondary
Sequence Homology, Amino Acid
Solutions
jenkins-FCD Prod-444 eb4ebd1a08581aba961d3befd3b851a3c3ec6b46