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.
Thermolysin is a well researched metallo protease containing <scene name='User:Ralf_Stephan/Sandbox_2/Zinc/2'>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 <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.
<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.<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>
==About this Structure==
2A7G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7G OCA].
==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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{{ABSTRACT_PUBMED_16131760}}
{{ABSTRACT_PUBMED_16131760}}
==About this Structure==
==References==
2A7G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7G OCA].
<references />
==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]
* 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]]
Revision as of 14:02, 7 February 2009
This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.
Classification and catalytic centerClassification and catalytic center
Thermolysin is a well researched metallo protease containing and several calcium atoms (yellow). The catalytic center consists of the HEXHH motif.
, holding it fast, while stabilize the substrate.[1][2]
On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection WavelengthOn the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength
↑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, Blomberg MR, Siegbahn PE. A theoretical study of the mechanism for peptide hydrolysis by thermolysin. J Biol Inorg Chem. 2002 Mar;7(3):284-98. Epub 2001 Sep 27. PMID:11935352 doi:http://dx.doi.org/10.1007/s007750100295
