This domain is composed of three alpha helices [1]. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation [2]. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins [3]. The domain is found to bind peptidoglycan experimentally [4]. This paper gives the crystal structure for this domain. However. no function is given for this domain.. [1]. 7121588. Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving. carboxypeptidase at 2.5 A resolution.. Dideberg O, Charlier P, Dive G, Joris B, Frere JM, Ghuysen JM;. Nature 1982;299:469-470.. [2]. 1683402. Cloning, expression, sequence analysis and biochemical. characterization of an autolytic amidase of Bacillus subtilis. 168 trpC2.. Foster SJ;. J Gen Microbiol 1991;137:1987-1998.. [3]. 7656014. The NMR structure of the inhibited catalytic domain of human. stromelysin-1.. Gooley PR, O'Connell JF, Marcy AI, Cuca GC, Salowe SP, Bush BL,. Hermes JD, Esser CK, Hagmann WK, Springer JP, et al;. Nat Struct Biol 1994;1:111-118.. [4]. 17697255. Muralytic activity and modular structure of the endolysins of. Pseudomonas aeruginosa bacteriophages phiKZ and EL.. Briers Y, Volckaert G, Cornelissen A, Lagaert S, Michiels CW,. Hertveldt K, Lavigne R;. Mol Microbiol. 2007;65:1334-1344. (from Pfam)
- Date:
- 2024-08-14