N Strater

Summary

Country: Germany

Publications

  1. pmc X-ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site-specific recombination
    N Strater
    Institut fur Kristallographie, Freie Universitat Berlin, Takustrasse 6, 14195 Berlin, Germany
    EMBO J 18:4513-22. 1999
  2. pmc A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase
    N Strater
    Institut fur Kristallographie, Freie Universitat Berlin, Takustrasse 6, D 14195 Berlin, Germany
    Proc Natl Acad Sci U S A 96:11151-5. 1999
  3. ncbi request reprint X-ray structure of acarbose bound to amylomaltase from Thermus aquaticus. Implications for the synthesis of large cyclic glucans
    I Przylas
    Institut für Chemie Kristallographie, Freie Universitat Berlin, Germany
    Eur J Biochem 267:6903-13. 2000
  4. ncbi request reprint Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures
    T Knöfel
    Institut fur Chemie, Abteilung Kristallographie, Freie Universitat Berlin, Germany
    J Mol Biol 309:239-54. 2001
  5. ncbi request reprint E. coli 5'-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion
    T Knöfel
    Institut fur Chemie, Abteilung Kristallographie, Freie Universitat Berlin, Germany
    J Mol Biol 309:255-66. 2001
  6. ncbi request reprint Crystal structure of amylomaltase from thermus aquaticus, a glycosyltransferase catalysing the production of large cyclic glucans
    I Przylas
    Freie Universitat Berlin, Institut fur Chemie, Abteilung Kristallographie, Takustrasse 6, Berlin, 14195, Germany
    J Mol Biol 296:873-86. 2000
  7. ncbi request reprint Crystallization and preliminary X-ray diffraction studies of the epsilonzeta addiction system encoded by Streptococcus pyogenes plasmid pSM19035
    A Meinhart
    Institut fur Kristallographie, Freie Universitat Berlin, Takustrasse 6, D 14195 Berlin, Germany
    Acta Crystallogr D Biol Crystallogr 57:745-7. 2001
  8. ncbi request reprint X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site
    T Knöfel
    Institut fur Kristallographie, Abteilung Saenger, Freie Universitat Berlin, Germany
    Nat Struct Biol 6:448-53. 1999

Collaborators

Detail Information

Publications8

  1. pmc X-ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site-specific recombination
    N Strater
    Institut fur Kristallographie, Freie Universitat Berlin, Takustrasse 6, 14195 Berlin, Germany
    EMBO J 18:4513-22. 1999
    ....
  2. pmc A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase
    N Strater
    Institut fur Kristallographie, Freie Universitat Berlin, Takustrasse 6, D 14195 Berlin, Germany
    Proc Natl Acad Sci U S A 96:11151-5. 1999
    ..A mutational analysis shows that Arg-356 influences activity by binding the bicarbonate ion but is not essential for activity. Mutation of the catalytic Lys-282 reduces k(cat)/K(m) about 10,000-fold...
  3. ncbi request reprint X-ray structure of acarbose bound to amylomaltase from Thermus aquaticus. Implications for the synthesis of large cyclic glucans
    I Przylas
    Institut für Chemie Kristallographie, Freie Universitat Berlin, Germany
    Eur J Biochem 267:6903-13. 2000
    ..The 250s loop might be involved in binding of the substrate at the reducing end of the scissile bond...
  4. ncbi request reprint Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures
    T Knöfel
    Institut fur Chemie, Abteilung Kristallographie, Freie Universitat Berlin, Germany
    J Mol Biol 309:239-54. 2001
    ..The site 1 metal ion coordinates a water molecule which is in an ideal position for a nucleophilic attack on the phosphorus atom, assuming an in-line mechanism of phosphoryl transfer. Another water molecule bridges the two metal ions...
  5. ncbi request reprint E. coli 5'-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion
    T Knöfel
    Institut fur Chemie, Abteilung Kristallographie, Freie Universitat Berlin, Germany
    J Mol Biol 309:255-66. 2001
    ..Few direct interdomain contacts and a layer of water molecules between the two domains facilitate the sliding motion...
  6. ncbi request reprint Crystal structure of amylomaltase from thermus aquaticus, a glycosyltransferase catalysing the production of large cyclic glucans
    I Przylas
    Freie Universitat Berlin, Institut fur Chemie, Abteilung Kristallographie, Takustrasse 6, Berlin, 14195, Germany
    J Mol Biol 296:873-86. 2000
    ..In amylomaltase, a conserved loop of around eight amino acid residues is partially shielding the active center. This loop, which is well conserved among other amylomaltases, may sterically hinder the formation of small cyclic products...
  7. ncbi request reprint Crystallization and preliminary X-ray diffraction studies of the epsilonzeta addiction system encoded by Streptococcus pyogenes plasmid pSM19035
    A Meinhart
    Institut fur Kristallographie, Freie Universitat Berlin, Takustrasse 6, D 14195 Berlin, Germany
    Acta Crystallogr D Biol Crystallogr 57:745-7. 2001
    ..9 A resolution and diffracted to 1.95 A after soaking at pH 7.0. A preparation of selenomethionyl epsilonzeta protein complex yielded single crystals suitable for X-ray diffraction experiments using synchrotron sources...
  8. ncbi request reprint X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site
    T Knöfel
    Institut fur Kristallographie, Abteilung Saenger, Freie Universitat Berlin, Germany
    Nat Struct Biol 6:448-53. 1999
    ....