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2G0Q

Solution structure of At5g39720.1 from Arabidopsis thaliana

Summary for 2G0Q
Entry DOI10.2210/pdb2g0q/pdb
NMR InformationBMRB: 7007
DescriptorAT5G39720.1 protein (1 entity in total)
Functional Keywordsat5g39720.1, structural genomics, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, unknown function
Biological sourceArabidopsis thaliana (thale cress)
Total number of polymer chains1
Total formula weight20126.82
Authors
Volkman, B.F.,Peterson, F.C.,Lytle, B.L.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2006-02-13, release date: 2006-02-28, Last modification date: 2024-05-29)
Primary citationLytle, B.L.,Peterson, F.C.,Tyler, E.M.,Newman, C.L.,Vinarov, D.A.,Markley, J.L.,Volkman, B.F.
Solution structure of Arabidopsis thaliana protein At5g39720.1, a member of the AIG2-like protein family.
Acta Crystallogr.,Sect.F, 62:490-493, 2006
Cited by
PubMed 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.
PubMed: 16754964
DOI: 10.1107/S1744309106015946
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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