4QRB

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

Summary for 4QRB

• Entry DOI: 10.2210/pdb4qrb/pdb
• Related: 4QR7 4QRA
• Descriptor: L,d-transpeptidase LdtB, GLCNAC(BETA1-4)-MURNAC(1,6-ANHYDRO)-L-ALA-GAMMA-D-GLU-MESO-A2PM-D-ALA (3 entities in total)
• Functional Keywords: 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, peptide cross linkage, peptidoglycan stems, bacterial cell wall periplasmic region, hydrolase
• Biological source: Mycobacterium tuberculosis
• Cellular location: Cell membrane ; Lipid-anchor : I6Y9J2
• Total number of polymer chains: 1
• Total formula weight: 38600.74

Authors

Gokulan, K.,Varughese, K.I. (deposition date: 2014-06-30, release date: 2015-12-23, Last modification date: 2024-02-28)

• 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 (1.64 Å)