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| <StructureSection load='2a7g' size='400' side='right' scene= caption='Thermolysin complex with acetate, DMS, Zn+2 (grey) and Ca+2 (green) ions, [[2a7g]]'> | | <StructureSection load='2a7g' size='350' side='right' scene= caption='Thermolysin complex with acetate, DMS, Zn+2 (grey) and Ca+2 (green) ions, [[2a7g]]'> |
| | == Function == |
| | [[Thermolysin]] or '''thermostable neutral proteinase''' (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. |
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| [[Image:2a7g.png|left|200px|thumb|Crystal Structure of Thermolysin [[2a7g]]]]
| | == 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>. |
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| [[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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| {{TOC limit|limit=2}}
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| == 3D Structures of Thermolysin == | | == 3D Structures of Thermolysin == |
| | | [[Thermolysin 3D structures]] |
| ''Update February 2013''
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| === Thermolysin ===
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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]] – TML<br /> | |
| [[3ls7]] - TML residues 233-548<br />
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| [[1trl]] - TML residues 255-316 – NMR<br />
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| [[3fxs]], [[3fbo]], [[3eim]], [[1lna]], [[1lnb]], [[1lnc]], [[1lnd]], [[1lne]], [[1lnf]] - TML residues 233-548+metal ion replacing Ca<br />
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| === TML+transition state analog ===
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| [[1tlp]], [[1tmn]], [[2tmn]], [[4tmn]], [[5tmn]] – TML+transition state analog<br />
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| ===TML+ amino acid===
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| [[1kl6]] – TML+ alanine<br />
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| [[3qgo]] – TML + phenylalanine methyl ester<br />
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| [[3qh1]] – TML + benzyloxycarboxyl- aspartate<br />
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| [[3qh5]] – TML + benzyloxycarboxyl- aspartate + phenylalanine methyl ester
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| === TML+ dipeptide ===
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| [[2wi0]], [[3tmn]] – TML+ dipeptide <br />
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| [[3fgd]] - TML residues 233-548+dipeptide<br />
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| === TML+inhibitor ===
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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 />
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| [[3fv4]], [[3fxp]], [[3flf]], [[3fb0]], [[3fcq]], [[3f28]], [[3f2p]] – TML residues 233-548+inhibitor<br />
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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]], [[3t73]], [[3t74]], [[3t87]], [[3t8c]], [[3t8d]], [[3t8f]], [[3t8g]], [[3t8h]], [[4h57]] – TML+inhibitor<br />
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| [[3ssb]] – TML + Impi-α<br />
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| [[3t2h]] – TML + trimethylamine oxide<br />
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| [[3t2i]] – TML + sarcosine<br />
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| [[3t2j]] – TML + betaine
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| </StructureSection> | | </StructureSection> |
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| ==References== | | == References == |
| <references /> | | <references/> |
| | | [[Category: Topic Page]] |
| [[Category:Topic Page]] | |
| [[Category: Bacillus thermoproteolyticus]]
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| [[Category: Single protein]]
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| [[Category: Transaldolase]]
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| [[Category: Mueller-Dieckmann, C.]]
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| [[Category: Panjikar, S.]]
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| [[Category: Tucker, P A.]]
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| [[Category: Weiss, M S.]]
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| [[Category: Transferase]]
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| <br />
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| Created with the participation of [[User:Ralf Stephan|Ralf Stephan]].
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