An ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation.

By G. Minasov, Xiaojun Wang, Brian K. Shoichet. 2002

204 citations recorded by the source corpus.

Subfields: Epidemiology, Molecular Biology, Molecular Medicine

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Martin Weigt
2. Matteo Figliuzzi
3. Alexander Schug
4. H. Jacquier
5. O. Tenaillon
6. Robert A. Bonomo
7. Sarah M. Drawz
8. Anne-Florence Bitbol

In Molecular Medicine

1. Robert A. Bonomo
2. Sarah M. Drawz

Citations in the corpus

• Coevolutionary Landscape Inference and the Context-Dependence of Mutations in Beta-Lactamase TEM-1 (2015, background): “These MSA contain the residue position carrying the mutation of interest, and all residues, which are, in a representative TEM-1 crystal structure (PDB: 1M40 [54]), within a distance dmax (we use the minimal distance between heavy atoms as the inter-residue distance).”
• Estimating the prevalence of protein sequences adopting functional enzyme folds. (2004, unknown): “fundamentally from the well-studied mechanism of class A b-lactamases.(15) A reasonable conjecture, in”
• Three Decades of β-Lactamase Inhibitors (2010, background): “Serine -lactamases acylate -lactam antibiotics, much like PBPs, and then use strategically positioned water molecules to hydrolyze the acylated -lactam (265).”