Thermolysin

spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D File:2a7g.png Crystal Structure of Thermolysin 2a7g Thermolysin (TML) is a thermostable metalloproteinase enzyme from Bacillus thermoproteolyticus. It catalyzes the hydrolysis of peptide bonds containing hydrophobic residues. The images at the left and at the right correspond to one representative Thermolysin (2a7g). Thermolysin is a well researched metalloprotease containing zinc (click this!) and the amino acids His-Glu-X-His-His as its catalytic center. Glu-166, His-142 and -146 are grouped around the zinc atom, holding it fast, while Glu-143 holds the polarized water atom. Additionally, Tyr-157 and His-231 stabilize the substrate protein which will be cleaved into two smaller proteins.. See Metalloproteases and Matrix metalloproteinase for discussion. 3D Structures of Thermolysin Update December 2011 Thermolysin 2whz, 3fvp, 3dnz, 3do0, 3do1, 3do2, 2g4z, 2a7g, 1gxw, 1kei, 1l3f, 1tlx, 2tlx, 8tln, 3p7p, 3p7q, 3p7r, 3p7s, 3p7t, 3p7u, 3p7v, 3p7w – TML 3ls7 - TML residues 233-548 1trl - TML residues 255-316 – NMR 3fxs, 3fbo, 3eim, 1lna, 1lnb, 1lnc, 1lnd, 1lne, 1lnf - TML residues 233-548+metal ion replacing Ca TML+transition state analog 1tlp, 1tmn, 2tmn, 4tmn, 5tmn – TML+transition state analog TML+ amino acid 1kl6 – TML+ alanine TML+ dipeptide 2wi0, 3tmn – TML+ dipeptide 3fgd - TML residues 233-548+dipeptide TML+inhibitor 1fjo, 1fj3, 1fjq, 1fjt, 1fju, 1fjv, 1fjw, 4tli, 5tli, 6tli, 7tli, 8tli, 1tli, 2tli, 3tli – TML soaked in organic solvents 3fv4, 3fxp, 3flf, 3fb0, 3fcq, 3f28, 3f2p – TML residues 233-548+inhibitor 3fwd, 3for, 1y3g, 1zdp, 1z9g, 1pes, 1pe7, 1pe8, 1os0, 1kto, 1ks7, 1kro, 1kr6, 1kkk, 1kjo, 1kjp, 1qf0, 1qf1, 1qf2, 1hyt, 1thl, 6tmn, 7tln, 4tln, 5tln, 1pe5, 3ms3, 3msa, 3msf, 3msn, 3n21, 3nn7 – TML+inhibitor 3ssb – TML + Impi-α

References

Created with the participation of Ralf Stephan.

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Alexander Berchansky, Michal Harel