4QR7

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

Summary for 4QR7

• Entry DOI: 10.2210/pdb4qr7/pdb
• Related: 4QRA 4QRB
• Descriptor: L,d-transpeptidase LdtB, GLCNAC(BETA1-4)-MURNAC(1,6-ANHYDRO)-L-ALA-GAMMA-D-GLU-MESO-A2PM-D-ALA, (2S,3R,4S)-4-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-2-[(2S,3R)-3-hydroxy-1-oxobutan-2-yl]-3-methyl-3,4-dihydro-2H-pyrrole-5-carboxylic acid, ... (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; single anomalous diffraction; imipenem; meropenem; peptidoglycan; beta-lactamase, hydrolase
• Biological source: Mycobacterium tuberculosis
• Cellular location: Cell membrane ; Lipid-anchor : I6Y9J2
• Total number of polymer chains: 1
• Total formula weight: 38986.22

Authors

Gokulan, K.,Varughese, K.I. (deposition date: 2014-06-30, release date: 2015-07-29, Last modification date: 2022-02-02)

• 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 (2.303 Å)