Sandbox Reserved 303

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=Thermolysin=
=Thermolysin=
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Thermolysin is a protein that is isolated from the thermophile ''Bacillus thermoproteolyticus''. <ref>Matthews. (1988).</ref> This protein is characterized by a remarkable stability under heat and protein denaturants. <ref>Vita et al., (1985).</ref> The structure does not contain any stabilizing disulfide bonds.<ref>Fontana et al., (1977).</ref> Instead, Thermolysin binds four calcium ions that are necessary for its thermal stability. <ref>Matthews. (1988).</ref>
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Thermolysin is a protein that is isolated from the thermophile ''Bacillus thermoproteolyticus''. <ref>Matthews. (1988).</ref> This protein is characterized by a remarkable stability under heat and protein denaturants. <ref>Vita et al., (1985).</ref> The structure does not contain any stabilizing disulfide bonds.<ref>Fontana et al., (1977).</ref> 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. <ref>Matthews. (1988).</ref>
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[http://ellen.warnerbros.com/ Ellen]
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One zinc ion is also present in the protein. This zinc ion is located at the active site of Thermolysin.<ref>Juers et al., (2005).</ref> 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. <ref>Matthews. (1988).</ref>
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{{STRUCTURE_1q8k|PDB=1q8k|SCENE=}}
{{STRUCTURE_1q8k|PDB=1q8k|SCENE=}}

Revision as of 06:48, 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. [4]

One zinc ion is also present in the protein. This zinc ion is located at the active site of Thermolysin.[5] 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. [6]




PDB ID 1q8k

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1q8k, 15 NMR models ()
Gene: EIF2S1 OR EIF2A (Homo sapiens)
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Works Cited

  1. ↑ Matthews. (1988).
  2. ↑ Vita et al., (1985).
  3. ↑ Fontana et al., (1977).
  4. ↑ Matthews. (1988).
  5. ↑ Juers et al., (2005).
  6. ↑ Matthews. (1988).
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