Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2F1E

Solution structure of ApaG protein

Summary for 2F1E
Entry DOI10.2210/pdb2f1e/pdb
NMR InformationBMRB: 5998
DescriptorProtein apaG (1 entity in total)
Functional Keywordsapag protein, xanthomonas axonopodis pv.citri, structural genomics, unknown function
Biological sourceXanthomonas axonopodis pv. citri
Total number of polymer chains1
Total formula weight14196.69
Authors
Contessa, G.,Pertinhez, T.A.,Spisni, A.,Paci, M.,Farah, C.S.,Cicero, D.O. (deposition date: 2005-11-14, release date: 2006-10-24, Last modification date: 2024-05-29)
Primary citationCicero, D.O.,Contessa, G.M.,Pertinhez, T.A.,Gallo, M.,Katsuyama, A.M.,Paci, M.,Farah, C.S.,Spisni, A.
Solution structure of ApaG from Xanthomonas axonopodis pv. citri reveals a fibronectin-3 fold.
Proteins, 67:490-500, 2007
Cited by
PubMed Abstract: ApaG proteins are found in a wide variety of bacterial genomes but their function is as yet unknown. Some eukaryotic proteins involved in protein-protein interactions, such as the human polymerase delta-interacting protein (PDIP38) and the F Box A (FBA) proteins, contain ApaG homology domains. We have used NMR to determine the solution structure of ApaG protein from the plant pathogen Xanthomonas axonopodis pv. citri (ApaG(Xac)) with the aim to shed some light on its molecular function. ApaG(Xac) is characterized by seven antiparallel beta strands forming two beta sheets, one containing three strands (ABE) and the other four strands (GFCC'). Relaxation measurements indicate that the protein has a quite rigid structure. In spite of the presence of a putative GXGXXG pyrophosphate binding motif ApaG(Xac) does not bind ATP or GTP, in vitro. On the other hand, ApaG(Xac) adopts a fibronectin type III (Fn3) fold, which is consistent with the hypothesis that it is involved in mediating protein-protein interactions. The fact that the proteins of ApaG family do not display significant sequence similarity with the Fn3 domains found in other eukaryotic or bacterial proteins suggests that Fn3 domain may have arisen earlier in evolution than previously estimated.
PubMed: 17256769
DOI: 10.1002/prot.21277
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

239803

数据于2025-08-06公开中

PDB statisticsPDBj update infoContact PDBjnumon