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1NMR

Solution Structure of C-terminal Domain from Trypanosoma cruzi Poly(A)-Binding Protein

Summary for 1NMR
Entry DOI10.2210/pdb1nmr/pdb
NMR InformationBMRB: 5698
Descriptorpoly(A)-binding protein (1 entity in total)
Functional Keywordsall helical domain, peptide binding protein
Biological sourceTrypanosoma cruzi
Total number of polymer chains1
Total formula weight9097.35
Authors
Siddiqui, N.,Kozlov, G.,D'Orso, I.,Trempe, J.F.,Frasch, A.C.C.,Gehring, K. (deposition date: 2003-01-10, release date: 2003-09-09, Last modification date: 2024-05-22)
Primary citationSiddiqui, N.,Kozlov, G.,D'Orso, I.,Trempe, J.F.,Gehring, K.
Solution Structure of the C-terminal Domain from poly(A)-binding protein in Trypanosoma cruzi: A vegetal PABC domain
Protein Sci., 12:1925-1933, 2003
Cited by
PubMed Abstract: PABC is a phylogenetically conserved peptide-binding domain primarily found within the C terminus of poly(A)-binding proteins (PABPs). This domain recruits a series of translation factors including poly(A)-interacting proteins (Paip1 and Paip2) and release factor 3 (RF3/GSPT) to the initiation complex on mRNA. Here, we determine the solution structure of the Trypanosoma cruzi PABC domain (TcPABC), a representative of the vegetal class of PABP proteins. TcPABC is similar to human PABC (hPABC) and consists of five alpha-helices, in contrast to the four helices observed in PABC domains from yeast (yPABC) and hyper plastic disk proteins (hHYD). A mobile N-terminal helix is observed in TcPABC that does not pack against the core of the protein, as found in hPABC. Characteristic to all PABC domains, the last four helices of TcPABC fold into a right-handed super coil. TcPABC demonstrates high-affinity binding to PABP interacting motif-2 (PAM-2) and reveals a peptide-binding surface homologous to that of hPABC. Our results demonstrate the last four helices in TcPABC are sufficient for peptide recognition and we predict a similar binding mode in PABC domains. Furthermore, these results point to the presence of putative PAM-2 site-containing proteins in trypanosomes.
PubMed: 12930992
DOI: 10.1110/ps.0390103
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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