4QTF

Structure and specificity of L-D-Transpeptidase from Mycobacterium tuberculosis and antibiotic resistance: Calcium binding promotes dimer formation

Summary for 4QTF

• Entry DOI: 10.2210/pdb4qtf/pdb
• Descriptor: L,d-transpeptidase LdtB, GLCNAC(BETA1-4)-MURNAC(1,6-ANHYDRO)-L-ALA-GAMMA-D-GLU-MESO-A2PM-D-ALA, (3S,5S)-3-({[(aminomethyl)amino]methyl}sulfanyl)-5-[(2S)-1,3-dioxobutan-2-yl]-L-proline, ... (4 entities in total)
• Functional Keywords: structural genomics, enzyme function initiative, center for structural genomics of infectious diseases, csgid, l-d-transpeptidase, d-d-transpeptidase, imipenem, meropenem, peptidoglycan, beta-lactamase, cross-linkage, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Mycobacterium tuberculosis
• Cellular location: Cell membrane ; Lipid-anchor : I6Y9J2
• Total number of polymer chains: 1
• Total formula weight: 38592.70

Authors

Gokulan, K.,Varughese, K.I. (deposition date: 2014-07-07, release date: 2015-07-29, Last modification date: 2023-09-20)

• Primary citation: Gokulan, K.,Khare, S.,Cerniglia, C.E.,Foley, S.L.,Varughese, K.I.; Structure and specificity of L-D-Transpeptidase from Mycobacterium tuberculosis and antibiotic resistance: Calcium binding promotes dimer formation; To be Published,

Experimental method

X-RAY DIFFRACTION (2 Å)