Thermolysin
From Proteopedia
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| - | [[Image: | + | [[Image:2a7g.png|left|200px|thumb|Crystal Structure of Thermolysin [[2a7g]]]] |
| - | {{ | + | {{STRUCTURE_2a7g| PDB=2a7g | SIZE=400| SCENE= |right|CAPTION=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 ([[ | + | [[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 [[metalloproteases|metalloprotease]] containing <scene name='User:Ralf_Stephan/Sandbox_2/Zinc/2'>zinc</scene> (click this!) and the amino acids His-Glu-X-His-His as its catalytic center. <scene name='User:Ralf_Stephan/Sandbox_2/Res_yellow/3'>Glu-166, His-142 and -146 are grouped around the zinc atom</scene>, holding it fast, while <scene name='User:Ralf_Stephan/Sandbox_2/Res/1'>Glu-143 holds the polarized water atom. Additionally, Tyr-157 and His-231</scene> stabilize the substrate protein which will be cleaved into two smaller proteins.<ref>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</ref><ref>PMID:11935352</ref>. See [[Metalloproteases]] and [[Matrix metalloproteinase]] for discussion. |
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[[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<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]] – TML+inhibitor<br /> | ||
[[3ssb]] – TML + Impi-α | [[3ssb]] – TML + Impi-α | ||
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| + | ==References== | ||
| + | <references /> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
| + | [[Category: Bacillus thermoproteolyticus]] | ||
| + | [[Category: Single protein]] | ||
| + | [[Category: Transaldolase]] | ||
| + | [[Category: Mueller-Dieckmann, C.]] | ||
| + | [[Category: Panjikar, S.]] | ||
| + | [[Category: Tucker, P A.]] | ||
| + | [[Category: Weiss, M S.]] | ||
| + | [[Category: Transferase]] | ||
| + | <br /> | ||
| + | Created with the participation of [[User:Ralf Stephan|Ralf Stephan]]. | ||
Revision as of 11:41, 6 June 2012
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
- ↑ 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
- ↑ 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.
