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/Center/1'>zinc</scene> and several calcium atoms (yellow). The catalytic center consists of the HEXHH motif.  
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]]

Revision as of 10:27, 7 February 2009

File:2a7g.png

Template:STRUCTURE 2a7g

Classification and catalytic center

Thermolysin is a well researched metallo protease containing zinc and several calcium atoms (yellow). The catalytic center consists of the HEXHH motif. Glu-166, His-142 and -146 are grouped around the zinc atom, holding it fast, while Glu-143 holds the polarized water atom. Additionally, Tyr-157 and His-231 stabilize the substrate.

On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength

Template:ABSTRACT PUBMED 16131760

About this Structure

2A7G is a Single protein structure of sequence from Bacillus thermoproteolyticus. Full crystallographic information is available from OCA.

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:16131760
  • Matthews, BW. (1988): Structural basis of the action of thermolysin and related zinc peptidases. In: Acc. Chem. Res. 21(9); 333–340; https://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; https://dx.doi.org/10.1007/s007750100295

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Ralf Stephan