Bioinformatics Discovery Note in Silico Identification of Putative Metal Binding Motifs

Metal ion binding domains are found in proteins that mediate transport, buffering or detoxification of metal ions. In this study, we have performed an in silico analysis of metal binding proteins and have identified putative metal binding motifs for the ions of cadmium, cobalt, zinc, arsenic, mercury, magnesium, manganese, molybdenum and nickel. A pattern search against the UniProtKB/Swiss-Prot and UniProtKB/TrEMBL databases yielded true positives in each case showing the high-specificity of the motifs. Motifs were also validated against PDB structures and site directed mutagenesis studies.

[1]  D. Hall,et al.  The high‐resolution crystal structure of the molybdate‐dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain folds , 1999, The EMBO journal.

[2]  C. Granqvist,et al.  Bacteria as workers in the living factory: metal-accumulating bacteria and their potential for materials science. , 2001, Trends in biotechnology.

[3]  U. Edlund,et al.  NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance. , 1998, Biochemistry.

[4]  J. D. Reid,et al.  Modification of cysteine residues in the ChlI and ChlH subunits of magnesium chelatase results in enzyme inactivation. , 2000, The Biochemical journal.

[5]  D. Nies,et al.  Energetics and Topology of CzcA, a Cation/Proton Antiporter of the Resistance-Nodulation-Cell Division Protein Family* , 1999, The Journal of Biological Chemistry.

[6]  S. Opella,et al.  Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system. , 1997, Biochemistry.

[7]  G J Barton,et al.  Identification of functional residues and secondary structure from protein multiple sequence alignment. , 1996, Methods in enzymology.

[8]  J. Okkeri,et al.  Introducing Wilson disease mutations into ZntA : Studies on the nucleotide and metal-binding sites of a bacterial zinc-translocating P-type ATPase , 2004 .

[9]  C. Rensing,et al.  Characteristics of Zinc Transport by Two Bacterial Cation Diffusion Facilitators from Ralstonia metallidurans CH34 and Escherichia coli , 2004, Journal of bacteriology.

[10]  J. Thompson,et al.  The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. , 1997, Nucleic acids research.

[11]  M. Steigerwald,et al.  Biosynthesis of cadmium sulphide quantum semiconductor crystallites , 1989, Nature.

[12]  Amos Bairoch,et al.  The PROSITE database, its status in 2002 , 2002, Nucleic Acids Res..

[13]  J. Powlowski,et al.  A Mercuric Ion Uptake Role for the Integral Inner Membrane Protein, MerC, Involved in Bacterial Mercuric Ion Resistance* , 1997, The Journal of Biological Chemistry.

[14]  Robert J.P. Williams,et al.  The Biological Chemistry of the Elements: The Inorganic Chemistry of Life , 2001 .

[15]  H. Mobley,et al.  Conserved Residues and Motifs in the NixA Protein ofHelicobacter pylori Are Critical for the High Affinity Transport of Nickel Ions* , 1998, The Journal of Biological Chemistry.

[16]  P. Kangueane,et al.  Molecular Basis for the Stereospecificity of Candida Rugosa Lipase (Crl) Towards Ibuprofen , 2000 .

[17]  A. Summers,et al.  Roles of the Tn21 merT, merP, and merC gene products in mercury resistance and mercury binding , 1992, Journal of bacteriology.

[18]  J. Omichinski,et al.  NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyase involved in the bacterial mercury resistance system. , 2004, Biochemistry.

[19]  R. Brennan,et al.  Structural basis for the metal-selective activation of the manganese transport regulator of Bacillus subtilis. , 2006, Biochemistry.

[20]  Gail J. Bartlett,et al.  Effective function annotation through catalytic residue conservation. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[21]  E. Pai,et al.  NmerA, the metal binding domain of mercuric ion reductase, removes Hg2+ from proteins, delivers it to the catalytic core, and protects cells under glutathione-depleted conditions. , 2005, Biochemistry.

[22]  Kumar,et al.  Extracellular biosynthesis of silver nanoparticles using the fungus Fusarium oxysporum , 2003 .

[23]  Zhilei Chen,et al.  A highly sensitive selection method for directed evolution of homing endonucleases , 2005, Nucleic acids research.

[24]  H. Schindelin,et al.  Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC. , 2000, Structure.

[25]  Sudhakar R. Sainkar,et al.  Fungus-mediated synthesis of silver nanoparticles and their immobilization in the mycelial matrix: a novel biological approach to nanoparticle synthesis , 2001 .

[26]  T. Haltia,et al.  Introducing Wilson disease mutations into the zinc-transporting P-type ATPase of Escherichia coli. The mutation P634L in the 'hinge' motif (GDGXNDXP) perturbs the formation of the E2P state. , 2002, European journal of biochemistry.

[27]  D. Nies,et al.  Microbial heavy-metal resistance , 1999, Applied Microbiology and Biotechnology.

[28]  R. Mehra,et al.  Metal ion resistance in fungi: Molecular mechanisms and their regulated expression , 1991, Journal of cellular biochemistry.

[29]  S. Basavaraja,et al.  Extracellular biosynthesis of silver nanoparticles using the fungus Fusarium semitectum , 2008 .

[30]  Amos Bairoch,et al.  ScanProsite: a reference implementation of a PROSITE scanning tool. , 2002, Applied bioinformatics.

[31]  C. Rensing,et al.  New functions for the three subunits of the CzcCBA cation-proton antiporter , 1997, Journal of bacteriology.

[32]  B. Edwards,et al.  Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme. , 2001, Structure.

[33]  D. Nies,et al.  Efflux-mediated heavy metal resistance in prokaryotes. , 2003, FEMS microbiology reviews.

[34]  M. Maguire,et al.  Emerging themes in manganese transport, biochemistry and pathogenesis in bacteria. , 2003, FEMS microbiology reviews.

[35]  J. Powlowski,et al.  Roles of the four cysteine residues in the function of the integral inner membrane Hg2+-binding protein, MerC. , 1999, Biochemical and biophysical research communications.

[36]  G. Pennathur,et al.  Effect of vegetable oils in the secretion of lipase from Candida rugosa (DSM 2031) , 1999 .

[37]  E Olsson,et al.  Silver-based crystalline nanoparticles, microbially fabricated. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[38]  R. Strange,et al.  XAFS studies of nitrogenase: the MoFe and VFe proteins and the use of crystallographic coordinates in three-dimensional EXAFS data analysis. , 2003, Journal of synchrotron radiation.

[39]  M H Saier,et al.  The RND permease superfamily: an ancient, ubiquitous and diverse family that includes human disease and development proteins. , 1999, Journal of molecular microbiology and biotechnology.

[40]  S. Silver Bacterial resistances to toxic metal ions--a review. , 1996, Gene.

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

[42]  Cheryl H Arrowsmith,et al.  Enzyme genomics: Application of general enzymatic screens to discover new enzymes. , 2005, FEMS microbiology reviews.

[43]  A. Belcher,et al.  Bacterial biosynthesis of cadmium sulfide nanocrystals. , 2004, Chemistry & biology.

[44]  D. Winge,et al.  Glutathione-coated cadmium-sulfide crystallites in Candida glabrata. , 1989, The Journal of biological chemistry.

[45]  F. Guillain,et al.  A Mutational Study in the Transmembrane Domain of Ccc2p, the Yeast Cu(I)-ATPase, Shows Different Roles for Each Cys-Pro-Cys Cysteine* , 2004, Journal of Biological Chemistry.

[46]  C. Vulpe,et al.  CPx-type ATPases: a class of P-type ATPases that pump heavy metals. , 1996, Trends in biochemical sciences.

[47]  D. Gatti,et al.  Conformational Changes in Four Regions of the Escherichia coli ArsA ATPase Link ATP Hydrolysis to Ion Translocation* , 2001, The Journal of Biological Chemistry.

[48]  Heather A H Haemig,et al.  Importance of Conserved Acidic Residues in MntH, the Nramp homolog of Escherichia coli , 2004, The Journal of Membrane Biology.

[49]  C. Sander,et al.  Are binding residues conserved? , 1998, Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing.

[50]  C. Rensing,et al.  Functional analysis of the Escherichia coli zinc transporter ZitB. , 2002, FEMS microbiology letters.

[51]  T. A. Krulwich,et al.  An antiport mechanism for a member of the cation diffusion facilitator family: divalent cations efflux in exchange for K+ and H+ , 2002, Molecular microbiology.

[52]  Itay Mayrose,et al.  Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues , 2002, ISMB.

[53]  N. Brown,et al.  The role of cysteine residues in the transport of mercuric ions by the Tn501 MerT and MerP mercury‐resistance proteins , 1995, Molecular microbiology.

[54]  M. Toledano,et al.  A Proteome Analysis of the Cadmium Response in Saccharomyces cerevisiae * , 2001, The Journal of Biological Chemistry.