Thermolysin: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
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>. | 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>. | ||
== 3D Structures of Thermolysin == | |||
[[Thermolysin 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
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*Thermolysin + amino acid | *Thermolysin + amino acid | ||
**[[1kl6]] – TML+ alanine<br /> | **[[1kl6]] – TML residues 1-316 + alanine<br /> | ||
**[[4m65]] – TML + asparagine<br /> | **[[4m65]] – TML residues 1-316 + asparagine<br /> | ||
**[[8tln]] – TML+ avaline + lysine<br /> | **[[8tln]] – TML+ avaline + lysine<br /> | ||
**[[3qgo]] – TML + phenylalanine methyl ester<br /> | **[[3qgo]] – TML + phenylalanine methyl ester<br /> | ||
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**[[3qh5]] – TML + benzyloxycarboxyl- aspartate + phenylalanine methyl ester | **[[3qh5]] – TML + benzyloxycarboxyl- aspartate + phenylalanine methyl ester | ||
*Thermolysin + | *Thermolysin + polypeptide | ||
**[[2wi0]], [[3tmn]], [[8tln]] – | **[[2wi0]], [[3tmn]], [[8tln]] – TMLresidues 1-316 + dipeptide <br /> | ||
**[[3fgd]] - TML residues 233-548+dipeptide<br /> | **[[3fgd]] - TML residues 233-548+dipeptide<br /> | ||
**[[5onp]], [[5onq]], [[5onr]], [[6ghx]] – TML residues 233-551 + amyloid-β peptide<br /> | |||
*Thermolysin + inhibitor | *Thermolysin + inhibitor | ||
**[[1fjo]], [[1fj3]], [[1fjq]], [[1fjt]], [[1fju]], [[1fjv]], [[1fjw]], [[4tli]], [[5tli]], [[6tli]], [[7tli]], [[8tli]], [[1tli]], [[2tli]], [[3tli]] – TML | **[[1fjo]], [[1fj3]], [[1fjq]], [[1fjt]], [[1fju]], [[1fjv]], [[1fjw]], [[4tli]], [[5tli]], [[6tli]], [[7tli]], [[8tli]], [[1tli]], [[2tli]], [[3tli]] – TML residues 1-316 in organic solvents<br /> | ||
**[[3fv4]], [[3fxp]], [[3flf]], [[3fb0]], [[3fcq]], [[3f28]], [[3f2p]], [[4mtw]], [[4mwp]], [[4mxj]], [[4mzn]], [[4n4e]], [[4n5p]], [[4n66]], [[4oi5]] | **[[3fv4]], [[3fxp]], [[3flf]], [[3fb0]], [[3fcq]], [[3f28]], [[3f2p]], [[4mtw]], [[4mwp]], [[4mxj]], [[4mzn]], [[4n4e]], [[4n5p]], [[4n66]], [[4oi5]], [[3for]], [[1y3g]], [[1zdp]], [[1z9g]], [[1os0]], [[1thl]], [[3ms3]], [[3msa]], [[3msf]], [[3msn]], [[3n21]], [[3nn7]], [[3t73]], [[3t74]], [[3t8]], [[3t8c]], [[3t8d]], [[3t8f]], [[3t8g]], [[3t8h]], [[4h57]], [[4d9w]], [[4d91]] – TML residues 233-548+inhibitor | ||
**[[1pe5]], [[6tmn]], [[7tln]], [[4tln]], [[5tln]], [[1hyt]], [[1qf0]], [[1qf1]], [[1qf2]], [[1kjp]], [[1kjo]], [[1kto]], [[1ks7]], [[1kro]], [[1kr6]], [[1kkk]], [[pe7]], [[1pe8]] – TML residues 1-316 + inhibitor <br /> | |||
**[[3ssb]] – TML + Impi-α<br /> | **[[3ssb]] – TML residues 233-548 + Impi-α<br /> | ||
**[[3t2h]] – TML + trimethylamine oxide<br /> | **[[3t2h]] – TML residues 233-548 + trimethylamine oxide<br /> | ||
**[[3t2i]] – TML + sarcosine<br /> | **[[3t2i]] – TML residues 233-548 + sarcosine<br /> | ||
**[[3t2j]] – TML + betaine<br /> | **[[3t2j]] – TML residues 233-548 + betaine<br /> | ||
**[[6fhp]] – TML C terminal 490-551 + DAIP<br /> | |||
**[[6fhp]] – TML C terminal + DAIP<br /> | |||
}} | }} | ||
Revision as of 11:02, 17 February 2020
FunctionThermolysin (TML) is a thermostable metalloproteinase enzyme from Bacillus thermoproteolyticus. It catalyzes the hydrolysis of peptide bonds containing hydrophobic residues. See Metalloproteases and Matrix metalloproteinase for discussion. Structural highlightsThermolysin 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]. 3D Structures of Thermolysin
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3D Structures of Thermolysin3D Structures of Thermolysin
Updated on 17-February-2020
ReferencesReferences
- ↑ 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