1kp0
From Proteopedia
(New page: 200px<br /><applet load="1kp0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kp0, resolution 2.7Å" /> '''The Crystal Structure...) |
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| - | [[Image:1kp0.jpg|left|200px]]<br /><applet load="1kp0" size=" | + | [[Image:1kp0.jpg|left|200px]]<br /><applet load="1kp0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kp0, resolution 2.7Å" /> | caption="1kp0, resolution 2.7Å" /> | ||
'''The Crystal Structure Analysis of Creatine Amidinohydrolase from Actinobacillus'''<br /> | '''The Crystal Structure Analysis of Creatine Amidinohydrolase from Actinobacillus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of Actinobacillus creatine amidinohydrolase has been | + | The crystal structure of Actinobacillus creatine amidinohydrolase has been solved by molecular replacement. The amino-acid sequence has been derived from the crystal structure. Crystals belong to space group I222, with unit-cell parameters a = 111.26 (3), b = 113.62 (4), c = 191.65 (2) A, and contain two molecules in an asymmetric unit. The structure was refined to an R factor of 18.8% at 2.7 A resolution. The crystal structure contains a dimer of 402 residues and 118 water molecules. The protein structure is bilobal, consisting of a small N-terminal domain and a large C-terminal domain. The C-terminal domain has a pitta-bread fold, similar to that found in Pseudomonas putida creatinase, proline aminopeptidases and methionine aminopeptidase. Comparison with complex crystal structures of P. putida creatinase reveals that the enzyme activity of Actinobacillus creatinase might be similar to that of P. putida creatinase. |
==About this Structure== | ==About this Structure== | ||
| - | 1KP0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Actinobacillus Actinobacillus]. Active as [http://en.wikipedia.org/wiki/Creatinase Creatinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.3 3.5.3.3] Full crystallographic information is available from [http:// | + | 1KP0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Actinobacillus Actinobacillus]. Active as [http://en.wikipedia.org/wiki/Creatinase Creatinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.3 3.5.3.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KP0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: alpha betal]] | [[Category: alpha betal]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:25 2008'' |
Revision as of 11:36, 21 February 2008
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The Crystal Structure Analysis of Creatine Amidinohydrolase from Actinobacillus
Overview
The crystal structure of Actinobacillus creatine amidinohydrolase has been solved by molecular replacement. The amino-acid sequence has been derived from the crystal structure. Crystals belong to space group I222, with unit-cell parameters a = 111.26 (3), b = 113.62 (4), c = 191.65 (2) A, and contain two molecules in an asymmetric unit. The structure was refined to an R factor of 18.8% at 2.7 A resolution. The crystal structure contains a dimer of 402 residues and 118 water molecules. The protein structure is bilobal, consisting of a small N-terminal domain and a large C-terminal domain. The C-terminal domain has a pitta-bread fold, similar to that found in Pseudomonas putida creatinase, proline aminopeptidases and methionine aminopeptidase. Comparison with complex crystal structures of P. putida creatinase reveals that the enzyme activity of Actinobacillus creatinase might be similar to that of P. putida creatinase.
About this Structure
1KP0 is a Single protein structure of sequence from Actinobacillus. Active as Creatinase, with EC number 3.5.3.3 Full crystallographic information is available from OCA.
Reference
Structure of creatine amidinohydrolase from Actinobacillus., Padmanabhan B, Paehler A, Horikoshi M, Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1322-8. Epub 2002, Jul 20. PMID:12136144
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