6T5L

MYO-1 from Myroides odoratimimus. Environmental metallo-beta-lactamases exhibit high enzymatic activity under zinc deprivation

Summary for 6T5L

• Entry DOI: 10.2210/pdb6t5l/pdb
• Descriptor: Subclass B1 metallo-beta-lactamase, ZINC ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: beta-lactamase, carbapenemase, environmental, metallo-beta-lactamase, mbl, antimicrobial protein
• Biological source: Myroides odoratimimus
• Total number of polymer chains: 2
• Total formula weight: 53922.22

Authors

Frohlich, C. (deposition date: 2019-10-16, release date: 2020-05-27, Last modification date: 2024-01-24)

Primary citation

Frohlich, C.,Sorum, V.,Huber, S.,Samuelsen, O.,Berglund, F.,Kristiansson, E.,Kotsakis, S.D.,Marathe, N.P.,Larsson, D.G.J.,Leiros, H.S.
Structural and biochemical characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1.
J.Antimicrob.Chemother., 75:2554-2563, 2020

PubMed Abstract: MBLs form a large and heterogeneous group of bacterial enzymes conferring resistance to β-lactam antibiotics, including carbapenems. A large environmental reservoir of MBLs has been identified, which can act as a source for transfer into human pathogens. Therefore, structural investigation of environmental and clinically rare MBLs can give new insights into structure-activity relationships to explore the role of catalytic and second shell residues, which are under selective pressure.

PubMed: 32464640
DOI: 10.1093/jac/dkaa175

Experimental method

X-RAY DIFFRACTION (2.17 Å)