“Open” structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase
- 1 September 2000
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 301 (5), 1257-1266
- https://doi.org/10.1006/jmbi.2000.3994
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- The Protein Data BankNucleic Acids Research, 2000
- Role of the Ortholog and Paralog Amino Acid Invariants in the Active Site of the UDP-MurNAc-l-alanine:d-glutamate Ligase (MurD)Biochemistry, 1999
- Determination of the MurD mechanism through crystallographic analysis of enzyme complexesJournal of Molecular Biology, 1999
- Crystallography & NMR System: A New Software Suite for Macromolecular Structure DeterminationActa Crystallographica Section D-Biological Crystallography, 1998
- ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletionsJournal of Applied Crystallography, 1997
- 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
- Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coliThe EMBO Journal, 1997
- Evaluation of the Kinetic Mechanism of Escherichia coli Uridine Diphosphate-N-acetylmuramate:l-Alanine LigaseBiochemistry, 1997
- Kinetic Mechanism of the Escherichia coli UDPMurNAc-Tripeptide d-Alanyl-d-alanine-Adding Enzyme: Use of a Glutathione S-Transferase FusionBiochemistry, 1996
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994