1qwy
From Proteopedia
|
Latent LytM at 1.3 A resolution
Overview
LytM, an autolysin from Staphylococcus aureus, is a Zn(2+)-dependent, glycyl-glycine endopeptidase with a characteristic HxH motif that belongs, to the lysostaphin-type (MEROPS M23/37) of metallopeptidases. Here, we, present the 1.3A crystal structure of LytM, the first structure of a, lysostaphin-type peptidase. In the LytM structure, the Zn(2+) is, tetrahedrally coordinated by the side-chains of N117, H210, D214 and H293, the second histidine of the HxH motif. Although close to the active-site, H291, the first histidine of the HxH motif, is not directly involved in, Zn(2+)-coordination, and there is no water molecule in the coordination, sphere of the Zn(2+), suggesting that the crystal structure shows a latent, form of the enzyme. Although LytM has not previously been considered as a, proenzyme, we show that a truncated version of LytM that lacks the, N-terminal part with the poorly conserved Zn(2+) ligand N117 has much, higher specific activity than full-length enzyme. This observation is, consistent with the known removal of profragments in other, lysostaphin-type proteins and with a prior observation of an active LytM, degradation fragment in S.aureus supernatant. The "asparagine switch" in, LytM is analogous to the "cysteine switch" in pro-matrix metalloproteases.
About this Structure
1QWY is a Single protein structure of sequence from Staphylococcus aureus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Latent LytM at 1.3A resolution., Odintsov SG, Sabala I, Marcyjaniak M, Bochtler M, J Mol Biol. 2004 Jan 16;335(3):775-85. PMID:14687573
Page seeded by OCA on Wed Nov 21 01:04:52 2007
