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-Structure paper
Title | Structure and specificity of L-D-Transpeptidase from Mycobacterium tuberculosis and antibiotic resistance: Calcium binding promotes dimer formation |
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Journal, issue, pages | To be Published |
Publish date | Jun 30, 2014 (structure data deposition date) |
![]() | Gokulan, K. / Khare, S. / Cerniglia, C.E. / Foley, S.L. / Varughese, K.I. |
![]() | Search PubMed |
Methods | X-ray diffraction |
Resolution | 1.64 - 2.303 Å |
Structure data | ![]() PDB-4qr7: ![]() PDB-4qra: ![]() PDB-4qrb: ![]() PDB-4qtf: |
Chemicals | ![]() ChemComp-MLD: ![]() ChemComp-DWZ: ![]() ChemComp-HOH: ![]() ChemComp-CA: ![]() ChemComp-3V5: |
Source |
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![]() | HYDROLASE / Structural Genomics / Enzyme Function Initiative / Center for Structural Genomics of Infectious Diseases / CSGID / L-D-transpeptidase; D-D-transpeptidase; Single anomalous diffraction; imipenem; meropenem; peptidoglycan; beta-lactamase / L-D-transpeptidase; D-D-transpeptidase; Single anomalous diffraction; imipenem; meropenem; / peptide cross linkage / peptidoglycan stems / Bacterial cell wall periplasmic region / HYDROLASE/HYDROLASE INHIBITOR / L-D-transpeptidase / D-D-transpeptidase / imipenem / meropenem / peptidoglycan / beta-lactamase / cross-linkage / HYDROLASE-HYDROLASE INHIBITOR complex |