Thermolysin

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Image:2a7g.png
Crystal Structure of Thermolysin 2a7g

Template:STRUCTURE 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 (click this!) and the amino acids His-Glu-X-His-His as its catalytic center. , holding it fast, while stabilize the substrate protein which will be cleaved into two smaller proteins.[1][2]. See Metalloproteases and Matrix metalloproteinase for discussion.

Contents

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

  1. ↑ Matthews, BW. (1988): Structural basis of the action of thermolysin and related zinc peptidases. In: Acc. Chem. Res. 21(9); 333–340; http://dx.doi.org/10.1021/ar00153a003
  2. ↑ Pelmenschikov V, Blomberg MR, Siegbahn PE. A theoretical study of the mechanism for peptide hydrolysis by thermolysin. J Biol Inorg Chem. 2002 Mar;7(3):284-98. Epub 2001 Sep 27. PMID:11935352 doi:http://dx.doi.org/10.1007/s007750100295


Created with the participation of Ralf Stephan.

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Michal Harel, Alexander Berchansky

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