5JWS

T4 Lysozyme L99A with 1-Hydro-2-ethyl-1,2-azaborine Bound

Summary for 5JWS

• Entry DOI: 10.2210/pdb5jws/pdb
• Related: 5JWT 5JWU 5JWV 5JWW 5JWX
• Descriptor: Endolysin, 2-ethyl-1,2-dihydro-1,2-azaborinine, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: phage lysozyme azaborine, hydrolase
• Biological source: Enterobacteria phage T4 sensu lato
• Cellular location: Host cytoplasm : P00720
• Total number of polymer chains: 1
• Total formula weight: 18764.15

Authors

Lee, H.,Fischer, M.,Shoichet, B.K.,Liu, S.-Y. (deposition date: 2016-05-12, release date: 2016-09-21, Last modification date: 2023-09-27)

Primary citation

Lee, H.,Fischer, M.,Shoichet, B.K.,Liu, S.Y.
Hydrogen Bonding of 1,2-Azaborines in the Binding Cavity of T4 Lysozyme Mutants: Structures and Thermodynamics.
J.Am.Chem.Soc., 138:12021-12024, 2016

PubMed Abstract: Protein crystallography and calorimetry were used to characterize the binding of 1,2-azaborines to model cavities in T4 lysozyme in direct comparison to their carbonaceous counterparts. In the apolar L99A cavity, affinity for Ab dropped only slightly versus benzene. In the cavity designed to accommodate a single hydrogen bond (L99A/M102Q), Gln102═O···H-N hydrogen bonding for Ab and BEtAb was observed in the crystallographic complexes. The strength of the hydrogen bonding was estimated as 0.94 and 0.64 kcal/mol for Ab and BEtAb, respectively. This work unambiguously demonstrates that 1,2-azaborines can be readily accommodated in classic aryl recognition pockets and establishes one of 1,2-azaborine's distinguishing features from its carbonaceous isostere benzene: its ability to serve as an NH hydrogen bond donor in a biological setting.

PubMed: 27603116
DOI: 10.1021/jacs.6b06566

Experimental method

X-RAY DIFFRACTION (1.65 Å)