CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships

Circular permutation of a protein can be visualized as if the original amino- and carboxyl termini were linked and new ones created elsewhere. It has been well-documented that circular permutants usually retain native structures and biological functions. Here we report CPSARST (Circular Permutation Search Aided by Ramachandran Sequential Transformation) to be an efficient database search tool. In this post-genomics era, when the amount of protein structural data is increasing exponentially, it provides a new way to rapidly detect novel relationships among proteins.

[1]  J. Quinn,et al.  Structure and kinetics of phosphonopyruvate hydrolase from Variovorax sp. Pal2: new insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily. , 2006, Biochemistry.

[2]  Patrice Koehl,et al.  The ASTRAL Compendium in 2004 , 2003, Nucleic Acids Res..

[3]  R. Tsien,et al.  Circular permutation and receptor insertion within green fluorescent proteins. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[4]  Jie Chen,et al.  Transition states for folding of circular‐permuted proteins , 2004, Proteins.

[5]  G M Edelman,et al.  Favin versus concanavalin A: Circularly permuted amino acid sequences. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[6]  Javier Santos,et al.  Mapping the distribution of conformational information throughout a protein sequence. , 2006, Journal of molecular biology.

[7]  Allegra Via,et al.  Local comparison of protein structures highlights cases of convergent evolution in analogous functional sites , 2007, BMC Bioinformatics.

[8]  W R Pearson,et al.  Flexible sequence similarity searching with the FASTA3 program package. , 2000, Methods in molecular biology.

[9]  J. Jung,et al.  Protein structure alignment using environmental profiles. , 2000, Protein engineering.

[10]  T. N. Bhat,et al.  The Protein Data Bank: unifying the archive , 2002, Nucleic Acids Res..

[11]  W. Delano The PyMOL Molecular Graphics System , 2002 .

[12]  U Heinemann,et al.  Circular permutations of protein sequence: not so rare? , 1995, Trends in biochemical sciences.

[13]  Kay Diederichs,et al.  Cation-π Interactions as Determinants for Binding of the Compatible Solutes Glycine Betaine and Proline Betaine by the Periplasmic Ligand-binding Protein ProX from Escherichia coli* , 2004, Journal of Biological Chemistry.

[14]  J. M. Sauder,et al.  Large‐scale comparison of protein sequence alignment algorithms with structure alignments , 2000, Proteins.

[15]  V. Bryson,et al.  Evolving Genes and Proteins. , 1965, Science.

[16]  T. Creighton,et al.  Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor. , 1983, Journal of molecular biology.

[17]  E. Myers,et al.  Basic local alignment search tool. , 1990, Journal of molecular biology.

[18]  J. Jung,et al.  Circularly permuted proteins in the protein structure database , 2001, Protein science : a publication of the Protein Society.

[19]  T. N. Bhat,et al.  The Protein Data Bank , 2000, Nucleic Acids Res..

[20]  Chih-Hung Chang,et al.  Protein structural similarity search by Ramachandran codes , 2007, BMC Bioinformatics.

[21]  Robert D. Finn,et al.  The Pfam protein families database , 2004, Nucleic Acids Res..

[22]  N. Grishin,et al.  Structurally analogous proteins do exist! , 2004, Structure.

[23]  D. Theobald,et al.  Divergent evolution within protein superfolds inferred from profile-based phylogenetics. , 2005, Journal of molecular biology.

[24]  R B Russell,et al.  Swaposins: circular permutations within genes encoding saposin homologues. , 1995, Trends in biochemical sciences.

[25]  E I Shakhnovich,et al.  Different circular permutations produced different folding nuclei in proteins: a computational study. , 2001, Journal of molecular biology.

[26]  L. Pauling,et al.  Evolutionary Divergence and Convergence in Proteins , 1965 .

[27]  C. Ramos,et al.  Circular permutation and deletion studies of myoglobin indicate that the correct position of its N-terminus is required for native stability and solubility but not for native-like heme binding and folding. , 2005, Biochemistry.

[28]  S. Pongor,et al.  Proteins of circularly permuted sequence present within the same organism: The major serine proteinase inhibitor from Capsicum annuum seeds , 2001, Protein science : a publication of the Protein Society.

[29]  Erich Bornberg-Bauer,et al.  Rapid motif-based prediction of circular permutations in multi-domain proteins , 2005, Bioinform..

[30]  Janusz M Bujnicki,et al.  Sequence permutations in the molecular evolution of DNA methyltransferases , 2002, BMC Evolutionary Biology.

[31]  A. Murzin Probable circular permutation in the flavin-binding domain , 1998, Nature Structural Biology.

[32]  J. Thompson,et al.  CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. , 1994, Nucleic acids research.

[33]  S. Verma,et al.  Structural stabilization of GTP-binding domains in circularly permuted GTPases: Implications for RNA binding , 2006, Nucleic Acids Research.

[34]  C. Sander,et al.  Protein structure comparison by alignment of distance matrices. , 1993, Journal of molecular biology.

[35]  C P Ponting,et al.  Protein fold irregularities that hinder sequence analysis. , 1998, Current opinion in structural biology.

[36]  S Uliel,et al.  Naturally occurring circular permutations in proteins. , 2001, Protein engineering.

[37]  T. Begley,et al.  Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II. , 2005, Biochemistry.

[38]  S. Henikoff,et al.  Amino acid substitution matrices from protein blocks. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[39]  D. Goldenberg,et al.  Alteration of the disulfide‐coupled folding pathway of BPTI by circular permutation , 2004, Protein science : a publication of the Protein Society.

[40]  Günter Blobel,et al.  Circular permutation as a tool to reduce surface entropy triggers crystallization of the signal recognition particle receptor β subunit , 2004, Protein science : a publication of the Protein Society.

[41]  J. Breed,et al.  Molecular determinants for substrate specificity of the ligand-binding protein OpuAC from Bacillus subtilis for the compatible solutes glycine betaine and proline betaine. , 2006, Journal of molecular biology.

[42]  Guoguang Lu,et al.  TOP: a new method for protein structure comparisons and similarity searches , 2000 .

[43]  Kenji Mizuguchi,et al.  A six-stranded double-psi β barrel is shared by several protein superfamilies , 1999 .

[44]  Zhiping Weng,et al.  FAST: A novel protein structure alignment algorithm , 2004, Proteins.

[45]  C. Orengo,et al.  Plasticity of enzyme active sites. , 2002, Trends in biochemical sciences.

[46]  D. Carrington,et al.  Polypeptide ligation occurs during post-translational modification of concanavalin A , 1985, Nature.

[47]  J. Rossjohn,et al.  Molecular basis of glutathione synthetase deficiency and a rare gene permutation event , 1999, The EMBO journal.

[48]  Zhen Qian,et al.  Improving the catalytic activity of Candida antarctica lipase B by circular permutation. , 2005, Journal of the American Chemical Society.

[49]  E V Koonin,et al.  Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains. , 2001, Journal of molecular biology.

[50]  G. Schneider,et al.  Circular permutations of natural protein sequences: structural evidence. , 1997, Current opinion in structural biology.

[51]  Marc Ostermeier,et al.  Engineering allosteric protein switches by domain insertion. , 2005, Protein engineering, design & selection : PEDS.

[52]  A. Galarneau,et al.  β-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein–protein interactions , 2002, Nature Biotechnology.

[53]  E. Bornberg-Bauer,et al.  Evolution of circular permutations in multidomain proteins. , 2006, Molecular biology and evolution.

[54]  Miki Kojima,et al.  Importance of terminal residues on circularly permutated Escherichia coli alkaline phosphatase with high specific activity. , 2005, Journal of bioscience and bioengineering.

[55]  William R. Taylor,et al.  Flexible Secondary Structure Based Protein Structure Comparison Applied to the Detection of Circular Permutation , 2006, J. Comput. Biol..

[56]  Albert Jeltsch,et al.  Circular Permutations in the Molecular Evolution of DNA Methyltransferases , 1999, Journal of Molecular Evolution.

[57]  Li-Chu Tsai,et al.  Crystal structure of a natural circularly permuted jellyroll protein: 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes. , 2003, Journal of molecular biology.

[58]  Michael Lappe,et al.  Prediction of viable circular permutants using a graph theoretic approach , 2006, Bioinform..

[59]  Stephen W Michnick,et al.  Beta-lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein protein interactions. , 2002, Nature biotechnology.

[60]  Luonan Chen,et al.  Revealing divergent evolution, identifying circular permutations and detecting active-sites by protein structure comparison , 2006, BMC Structural Biology.

[61]  Dan S. Tawfik,et al.  Evolution of new protein topologies through multistep gene rearrangements , 2006, Nature Genetics.

[62]  T L Blundell,et al.  A six-stranded double-psi beta barrel is shared by several protein superfamilies. , 1999, Structure.

[63]  Anil K. Jain,et al.  Algorithms for Clustering Data , 1988 .

[64]  Amihood Amir,et al.  A simple algorithm for detecting circular permutations in proteins , 1999, Bioinform..

[65]  C. Vogel,et al.  Duplication, divergence and formation of novel protein topologies. , 2006, BioEssays : news and reviews in molecular, cellular and developmental biology.

[66]  A. Brunger,et al.  Structural Basis of Rab Effector Specificity Crystal Structure of the Small G Protein Rab3A Complexed with the Effector Domain of Rabphilin-3A , 1999, Cell.

[67]  P E Bourne,et al.  Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. , 1998, Protein engineering.

[68]  S F Altschul,et al.  Local alignment statistics. , 1996, Methods in enzymology.

[69]  K. Diederichs,et al.  Structural Basis for the Binding of Compatible Solutes by ProX from the Hyperthermophilic Archaeon Archaeoglobus fulgidus* , 2004, Journal of Biological Chemistry.