Crystal structure of a thermophilic GrpE protein: insight into thermosensing function for the DnaK chaperone system.

[1]  A. Brunger.  Version 1.2 of the Crystallography and NMR system , 2007, Nature Protocols.

[2]  K. Harata,et al.  Implication for buried polar contacts and ion pairs in hyperthermostable enzymes , 2007, The FEBS journal.

[3]  S. Yokoyama,et al.  Hyper‐thermostability of CutA1 protein, with a denaturation temperature of nearly 150 °C , 2006 .

[4]  Jonathan Weissman,et al.  Molecular Chaperones and Protein Quality Control , 2006, Cell.

[5]  W. Stafford,et al.  Thermodynamic linkage in the GrpE nucleotide exchange factor, a molecular thermosensor. , 2003, Biochemistry.

[6]  W. Stafford,et al.  A structure-based interpretation of E.coli GrpE thermodynamic properties. , 2002, Journal of molecular biology.

[7]  S. Schlee,et al.  The DnaK/ClpB chaperone system from Thermus thermophilus , 2002, Cellular and Molecular Life Sciences CMLS.

[8]  F. Hartl,et al.  Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein , 2002, Science.

[9]  Y. Groemping,et al.  Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response. , 2001, Journal of molecular biology.

[10]  P. Christen,et al.  Reversible Thermal Transition in GrpE, the Nucleotide Exchange Factor of the DnaK Heat-Shock System* , 2001, The Journal of Biological Chemistry.

[11]  S. N. Witt,et al.  GrpE accelerates peptide binding and release from the high affinity state of DnaK , 2001, Nature Structural Biology.

[12]  C. Vieille,et al.  Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability , 2001, Microbiology and Molecular Biology Reviews.

[13]  J. Reinstein,et al.  Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE. , 2001, Journal of molecular biology.

[14]  R. Seidel,et al.  The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system. , 1999, Journal of molecular biology.

[15]  Thomas C. Terwilliger,et al.  Automated MAD and MIR structure solution , 1999, Acta crystallographica. Section D, Biological crystallography.

[16]  R J Read,et al.  Crystallography & NMR system: A new software suite for macromolecular structure determination. , 1998, Acta crystallographica. Section D, Biological crystallography.

[17]  Bernd Bukau,et al.  The Hsp70 and Hsp60 Chaperone Machines , 1998, Cell.

[18]  A. Vagin,et al.  MOLREP: an Automated Program for Molecular Replacement , 1997 .

[19]  J Kuriyan,et al.  Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. , 1997, Science.

[20]  J. Reinstein,et al.  GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. , 1997, Biochemistry.

[21]  Masasuke Yoshida,et al.  A Novel Factor Required for the Assembly of the DnaK and DnaJ Chaperones of Thermus thermophilus* , 1996, The Journal of Biological Chemistry.

[22]  N. Dohmae,et al.  Characterization of a thermostable lysine-specific metalloendopeptidase from the fruiting bodies of a basidiomycete, Grifola frondosa. , 1995, Journal of biochemistry.

[23]  Collaborative Computational,et al.  The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.

[24]  A. Lupas,et al.  Predicting coiled coils from protein sequences , 1991, Science.

[25]  W. Kabsch,et al.  Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.

[26]  B. Matthews.  Solvent content of protein crystals. , 1968, Journal of molecular biology.

[27]  Jack Snoeyink,et al.  Nucleic Acids Research Advance Access published April 22, 2007 MolProbity: all-atom contacts and structure validation for proteins and nucleic acids , 2007 .

[28]  S. Yokoyama,et al.  Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150 degrees C. , 2006, FEBS letters.

[29]  P. Afonine,et al.  research papers Acta Crystallographica Section D Biological , 2003 .

[30]  C. Harrison.  GrpE, a nucleotide exchange factor for DnaK , 2003, Cell stress & chaperones.

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

[32]  Z. Otwinowski,et al.  Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.

[33]  J T Yang,et al.  Calculation of protein conformation from circular dichroism. , 1986, Methods in enzymology.

[34]  Thomas C. Terwilliger,et al.  Electronic Reprint Biological Crystallography Maximum-likelihood Density Modification , 2022 .