+ Site Statistics
References:
54,258,434
Abstracts:
29,560,870
PMIDs:
28,072,757
+ Search Articles
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ PDF Full Text
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Translate
+ Recently Requested

Identification of a novel calcium binding motif based on the detection of sequence insertions in the animal peroxidase domain of bacterial proteins



Identification of a novel calcium binding motif based on the detection of sequence insertions in the animal peroxidase domain of bacterial proteins



Plos One 7(7): E40698



Proteins of the animal heme peroxidase (ANP) superfamily differ greatly in size since they have either one or two catalytic domains that match profile PS50292. The orf PP_2561 of Pseudomonas putida KT2440 that we have called PepA encodes a two-domain ANP. The alignment of these domains with those of PepA homologues revealed a variable number of insertions with the consensus G-x-D-G-x-x-[GN]-[TN]-x-D-D. This motif has also been detected in the structure of pseudopilin (pdb 3G20), where it was found to be involved in Ca(2+) coordination although a sequence analysis did not reveal the presence of any known calcium binding motifs in this protein. Isothermal titration calorimetry revealed that a peptide containing this consensus motif bound specifically calcium ions with affinities ranging between 33-79 µM depending on the pH. Microcalorimetric titrations of the purified N-terminal ANP-like domain of PepA revealed Ca(2+) binding with a K(D) of 12 µM and stoichiometry of 1.25 calcium ions per protein monomer. This domain exhibited peroxidase activity after its reconstitution with heme. These data led to the definition of a novel calcium binding motif that we have termed PERCAL and which was abundantly present in animal peroxidase-like domains of bacterial proteins. Bacterial heme peroxidases thus possess two different types of calcium binding motifs, namely PERCAL and the related hemolysin type calcium binding motif, with the latter being located outside the catalytic domains and in their C-terminal end. A phylogenetic tree of ANP-like catalytic domains of bacterial proteins with PERCAL motifs, including single domain peroxidases, was divided into two major clusters, representing domains with and without PERCAL motif containing insertions. We have verified that the recently reported classification of bacterial heme peroxidases in two families (cd09819 and cd09821) is unrelated to these insertions. Sequences matching PERCAL were detected in all kingdoms of life.

(PDF emailed within 1 workday: $29.90)

Accession: 053661610

Download citation: RISBibTeXText

PMID: 22808235


Related references

A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation. Embo Journal 22(8): 1743-1752, 2003

PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine. Science 268(5214): 1177-1179, 1995

Identification of a novel protein sequence motif The RAN GTPase binding domain. Journal of Cellular Biochemistry Supplement 0(19A): 55, 1995

Identification of two Entamoeba histolytica sequence-specific URE4 enhancer-binding proteins with homology to the RNA-binding motif RRM. Journal of Biological Chemistry 276(2): 1602-1609, 2000

The Ran/TC4 GTPase-binding domain: identification by expression cloning and characterization of a conserved sequence motif. Proceedings of the National Academy of Sciences of the United States of America 92(8): 3328-3332, 1995

SSMART: sequence-structure motif identification for RNA-binding proteins. Bioinformatics 34(23): 3990-3998, 2018

Membrane domain formation by calcium-dependent, lipid-binding proteins: insights from the C2 motif. Biochimica et Biophysica Acta 1448(2): 227-235, 1999

Membrane domain formation by calcium-dependent, lipid-binding proteins: Insights from the C2 motif. Biochimica et Biophysica Acta 1448(2): 227-235, Dec 10, 1998

Identification of a mouse orthologue of the human ras-GAP-SH3-domain binding protein and structural confirmation that these proteins contain an RNA recognition motif. Biomedical Peptides, Proteins and Nucleic Acids 2(3): 93-99, 1996

Homology of a conserved sequence in the tail domain of intermediate filament proteins with the loop region of calcium binding proteins. Cell Biology International Reports 11(11): 831, 1987

A putative Src homology 3 domain binding motif but not the C-terminal dystrophin WW domain binding motif is required for dystroglycan function in cellular polarity in Drosophila. Journal of Biological Chemistry 282(20): 15159-15169, 2007

The iq motif a putative consensus sequence for calmodulin binding sites that function in the absence of calcium is present in many different proteins including myosins neuromodulin neurogranin pep 19 and cavpt. Journal of Cell Biology 115(3 PART 2): 432A, 1991

Inhibition of NADPH oxidase activation by synthetic peptides mapping within the carboxyl-terminal domain of small GTP-binding proteins. Lack of amino acid sequence specificity and importance of polybasic motif. Journal of Biological Chemistry 269(46): 29024-29031, 1994

Tyrosine phosphorylation of b-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins. Biochemistry (American Chemical Society) 40(48): 585-92, 2001

Yeast protein-protein interaction binding sites: prediction from the motif-motif, motif-domain and domain-domain levels. Molecular Biosystems 6(11): 2164-2173, 2011