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-	{{STRUCTURE_1q8k|PDB=1q8k|SCENE=}}	+	{{STRUCTURE_1y3g|PDB=1y3g|SCENE=}}
-	<scene name='Sandbox_Reserved_303/Elf/2'>coolest fish in the sea.</scene>	+	<scene name='Sandbox_Reserved_303/Thermolysin'>Thermolysin.</scene>
	=Works Cited=		=Works Cited=
	<references/>		<references/>

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Revision as of 07:32, 12 March 2011

This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.

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Thermolysin

Thermolysin is a protein that is isolated from the thermophile Bacillus thermoproteolyticus. ^[1] This protein is characterized by a remarkable stability under heat and protein denaturants. ^[2] The structure does not contain any stabilizing disulfide bonds.^[3] Instead, Thermolysin binds four calcium ions that are necessary for its thermal stability. These four ions increase the intrinsic thermostability of the protein and protect its surface loops against autolysis. ^[1]

One zinc ion is also present in the protein. This zinc ion is located at the active site of Thermolysin.^[4] This molecule is essential for the enzyme's function. The zinc ion exists in an approximate tetrahedral coordination, bound to three amino acids (HIS 142, HIS 146, GLU 166) and water. During its activity, an incoming substrate will displace this water molecule towards GLU 143. ^[1] GLU 143 is thought to help activate this same water molecule, which will attack the substrate.^[4]

The zinc ion activates the scissile amide bond towards attack by water and stabilizes the resulting tetrahedral intermediate.^[4] The metal is able to react with a number of functional groups that act as inhibitors. Some of these groups include thiols, ketones, hydroxamic acids, anionic groups such as carboxylates ans phosphinates, and silanediols.^[4] The design of metalloprotease inhibitors such as for thermolysin is a common pharmaceutical target.^[4]

Thermolysin was one of the first metalloproteases to have its structure solved crystallographically.^[4]

spinqualitylabelsall models PDB ID 1y3g Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1y3g, resolution 2.10Å ()
Ligands:	, , ,
Non-Standard Residues:
Activity:	Thermolysin, with EC number 3.4.24.27
Structural annotation: Resources: CATH : 1Y3Ge02, 1Y3Ge01 InterPro : Ipr013832, Ipr006025, Ipr013856, Ipr011096, Ipr001570, Ipr005075 Pfam : PF01447, PF02868 UniProt : P00800
Functional annotation: Cellular component: extracellular region Biological process: proteolysis Molecular function: hydrolase activity metalloendopeptidase activity metal ion binding zinc ion binding calcium ion binding metallopeptidase activity peptidase activity
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

Works Cited

1. ↑ ^{1.0 1.1 1.2} Matthews. (1988).
2. ↑ Vita et al., (1985).
3. ↑ Fontana et al., (1977).
4. ↑ ^{4.0 4.1 4.2 4.3 4.4 4.5} Juers et al., (2005).