User:Ralf Stephan/Sandbox 2

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== Classification and catalytic center ==
== Classification and catalytic center ==
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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.
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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.
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<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.
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<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>
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==About this Structure==
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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}}
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==About this Structure==
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==References==
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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].
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<references />
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==Reference==
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*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]
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* 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
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* 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
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[[Category: Bacillus thermoproteolyticus]]
[[Category: Bacillus thermoproteolyticus]]

Revision as of 11:02, 7 February 2009

Image:2a7g.png

Template:STRUCTURE 2a7g

Contents

Classification 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]

About this Structure

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

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

Template:ABSTRACT PUBMED 16131760

References

  1. ↑ 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
  2. ↑ 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

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Ralf Stephan

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