Structural and functional similarities in the ADP-forming amide bond ligase superfamily: implications for a substrate-induced conformational change in folylpolyglutamate synthetase
- 15 September 2000
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 302 (2) , 425-438
- https://doi.org/10.1006/jmbi.2000.3987
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Identification of Three Key Active Site Residues in the C-terminal Domain of Human Recombinant Folylpoly-γ-glutamate Synthetase by Site-directed MutagenesisJournal of Biological Chemistry, 1999
- Determination of the MurD mechanism through crystallographic analysis of enzyme complexesJournal of Molecular Biology, 1999
- Invariant Amino Acids in the Mur Peptide Synthetases of Bacterial Peptidoglycan Synthesis and Their Modification by Site-Directed Mutagenesis in the UDP-MurNAc:l-Alanine Ligase from Escherichia coliBiochemistry, 1997
- Conditionally Lethal Escherichia coli Murein Mutants Contain Point Defects That Map to Regions Conserved among Murein and Folyl Poly-γ-glutamate Ligases: Identification of a Ligase SuperfamilyBiochemistry, 1997
- Study of the Reaction Mechanism of thed-Glutamic Acid-Adding Enzyme fromEscherichia coliMicrobial Drug Resistance, 1996
- Mechanistic implications and family relationships from the structure of dethiobiotin synthetaseStructure, 1994
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- MOLSCRIPT: a program to produce both detailed and schematic plots of protein structuresJournal of Applied Crystallography, 1991
- The P-loop — a common motif in ATP- and GTP-binding proteinsTrends in Biochemical Sciences, 1990
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977