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Structure paper

TitleAllosteric cooperation in beta-lactam binding to a non-classical transpeptidase.
Journal, issue, pagesElife, Vol. 11, Year 2022
Publish dateJun 26, 2021 (structure data deposition date)
AuthorsAhmad, N. / Dugad, S. / Chauhan, V. / Ahmed, S. / Sharma, K. / Kachhap, S. / Zaidi, R. / Bishai, W.R. / Lamichhane, G. / Kumar, P.
External linksElife / PubMed:35475970
MethodsX-ray diffraction
Resolution1.58 - 1.7 Å
Structure data

PDB-7f71:
Crystal structure of the Mycobacterium tuberculosis L,D-transpeptidase-2 (LdtMt2) with peptidoglycan sugar moiety and glutamate
Method: X-RAY DIFFRACTION / Resolution: 1.58 Å

PDB-7f8p:
Crystal structure of the Mycobacterium tuberculosis L,D-transpeptidase-2 (LdtMt2) with new carbapenem drug T203
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-GLU:
GLUTAMIC ACID

ChemComp-BGC:
beta-D-glucopyranose

ChemComp-HOH:
WATER

ChemComp-59I:
(2R,3R)-3-methyl-4-(2-oxidanylidene-2-propan-2-yloxy-ethyl)sulfanyl-2-[(2R)-3-oxidanyl-1-oxidanylidene-butan-2-yl]-2,3-dihydro-1H-pyrrole-5-carboxylic acid

ChemComp-56X:
(4R,5S,6S)-6-((R)-1-hydroxyethyl)-3-((2-isopropoxy-2-oxoethyl)thio)-4-methyl-7-oxo-1-azabicyclo[3.2.0]hept-2-ene-2-carboxylic acid

Source
  • mycobacterium tuberculosis (strain atcc 25618 / h37rv) (bacteria)
KeywordsHYDROLASE / L / D-transpeptidase / Cysteine protease

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