User:Ralf Stephan/Sandbox 2: Difference between revisions
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== Classification and catalytic center == | == Classification and catalytic center == | ||
Thermolysin is a well researched metallo protease containing <scene name='User:Ralf_Stephan/Sandbox_2/ | Thermolysin is a well researched metallo protease containing <scene name='User:Ralf_Stephan/Sandbox_2/Zinc/1'>zinc</scene> and several calcium atoms (yellow). The catalytic center consists of the HEXHH motif. | ||
<scene name='User:Ralf_Stephan/Sandbox_2/Res_yellow/2'>Glu-166, His-142 and -146 are grouped around the zinc atom</scene>, holding it fast, while Glu-143 holds the polarized water atom. Additionally, Tyr-157 and His-231 stabilize the substrate. | <scene name='User:Ralf_Stephan/Sandbox_2/Res_yellow/2'>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_orange/1'>Glu-143 holds the polarized water atom. Additionally, Tyr-157 and His-231</scene> stabilize the substrate. | ||
==On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength== | ==On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength== | ||
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==Reference== | ==Reference== | ||
On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength., Mueller-Dieckmann C, Panjikar S, Tucker PA, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1263-72. Epub 2005, Aug 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16131760 16131760] | *On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength., Mueller-Dieckmann C, Panjikar S, Tucker PA, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1263-72. Epub 2005, Aug 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16131760 16131760] | ||
* 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. ''et al.'' (2002): ''A theoretical study of the mechanism for peptide hydrolysis by thermolysin''. ''J Biol Inorg Chem.'' '''7'''(3); 284–98; PMID:11935352; http://dx.doi.org/10.1007/s007750100295 | |||
[[Category: Bacillus thermoproteolyticus]] | [[Category: Bacillus thermoproteolyticus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
