Thermolysin: Difference between revisions

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[[2whz]], [[3fvp]], [[3dnz]], [[3do0]], [[3do1]], [[3do2]], [[2g4z]], [[2a7g]], [[1gxw]], [[1kei]], [[1l3f]], [[1tlx]], [[2tlx]], [[8tln]], [[3p7p]], [[3p7q]], [[3p7r]], [[3p7s]], [[3p7t]], [[3p7u]], [[3p7v]], [[3p7w]], [[3zi6]] – TML<br />
[[2whz]], [[3fvp]], [[3dnz]], [[3do0]], [[3do1]], [[3do2]], [[2g4z]], [[2a7g]], [[1gxw]], [[1kei]], [[1l3f]], [[1tlx]], [[2tlx]], [[8tln]], [[3p7p]], [[3p7q]], [[3p7r]], [[3p7s]], [[3p7t]], [[3p7u]], [[3p7v]], [[3p7w]], [[3zi6]] – TML<br />
[[3ls7]] - TML residues 233-548<br />
[[3ls7]], [[4ow3]] - TML residues 233-548<br />
[[1trl]] - TML residues 255-316 – NMR<br />
[[1trl]] - TML residues 255-316 – NMR<br />
[[3fxs]], [[3fbo]], [[3eim]], [[1lna]], [[1lnb]], [[1lnc]], [[1lnd]], [[1lne]], [[1lnf]] - TML residues 233-548+metal ion replacing Ca<br />
[[3fxs]], [[3fbo]], [[3eim]], [[1lna]], [[1lnb]], [[1lnc]], [[1lnd]], [[1lne]], [[1lnf]] - TML residues 233-548+metal ion replacing Ca<br />
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[[1kl6]] – TML+ alanine<br />
[[1kl6]] – TML+ alanine<br />
[[4m65]] – TML + asparagine<br />
[[3qgo]] – TML + phenylalanine methyl ester<br />
[[3qgo]] – TML + phenylalanine methyl ester<br />
[[3qh1]] – TML + benzyloxycarboxyl- aspartate<br />
[[3qh1]] – TML + benzyloxycarboxyl- aspartate<br />
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[[1fjo]], [[1fj3]], [[1fjq]], [[1fjt]], [[1fju]], [[1fjv]], [[1fjw]], [[4tli]], [[5tli]], [[6tli]], [[7tli]], [[8tli]], [[1tli]], [[2tli]], [[3tli]] – TML soaked in organic solvents<br />
[[1fjo]], [[1fj3]], [[1fjq]], [[1fjt]], [[1fju]], [[1fjv]], [[1fjw]], [[4tli]], [[5tli]], [[6tli]], [[7tli]], [[8tli]], [[1tli]], [[2tli]], [[3tli]] – TML soaked in organic solvents<br />
[[3fv4]], [[3fxp]], [[3flf]], [[3fb0]], [[3fcq]], [[3f28]], [[3f2p]] – TML residues 233-548+inhibitor<br />
[[3fv4]], [[3fxp]], [[3flf]], [[3fb0]], [[3fcq]], [[3f28]], [[3f2p]], [[4mtw]], [[4mwp]], [[4mxj]], [[4mzn]], [[4n4e]], [[4n5p]], [[4n66]], [[4oi5]] – TML residues 233-548+inhibitor<br />
[[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]], [[3t73]], [[3t74]], [[3t87]], [[3t8c]], [[3t8d]], [[3t8f]], [[3t8g]], [[3t8h]], [[4h57]], [[4d9w]], [[4d91]] – TML+inhibitor<br />
[[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]], [[3t73]], [[3t74]], [[3t87]], [[3t8c]], [[3t8d]], [[3t8f]], [[3t8g]], [[3t8h]], [[4h57]], [[4d9w]], [[4d91]] – TML+inhibitor<br />
[[3ssb]] – TML + Impi-α<br />
[[3ssb]] – TML + Impi-α<br />

Revision as of 12:21, 18 May 2014


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 (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.

3D Structures of Thermolysin

Updated on 30-May-2025

Thermolysin

2whz, 3fvp, 3dnz, 3do0, 3do1, 3do2, 2g4z, 2a7g, 1gxw, 1kei, 1l3f, 1tlx, 2tlx, 8tln, 3p7p, 3p7q, 3p7r, 3p7s, 3p7t, 3p7u, 3p7v, 3p7w, 3zi6 – TML

3ls7, 4ow3 - 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

4m65 – TML + asparagine
3qgo – TML + phenylalanine methyl ester
3qh1 – TML + benzyloxycarboxyl- aspartate
3qh5 – TML + benzyloxycarboxyl- aspartate + phenylalanine methyl ester

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, 4mtw, 4mwp, 4mxj, 4mzn, 4n4e, 4n5p, 4n66, 4oi5 – 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, 3t73, 3t74, 3t87, 3t8c, 3t8d, 3t8f, 3t8g, 3t8h, 4h57, 4d9w, 4d91 – TML+inhibitor
3ssb – TML + Impi-α
3t2h – TML + trimethylamine oxide
3t2i – TML + sarcosine
3t2j – TML + betaine


PDB ID 2a7g

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ReferencesReferences

  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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Alexander Berchansky, Michal Harel