1kp0: Difference between revisions

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[[Image:1kp0.~~jpg~~|left|200px]]

[[Image:1kp0.png|left|200px]]

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~~'''~~The Crystal Structure Analysis of Creatine Amidinohydrolase from Actinobacillus~~'''~~

===The Crystal Structure Analysis of Creatine Amidinohydrolase from Actinobacillus===

~~==Overview==~~

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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.

The line below this paragraph, {{ABSTRACT_PUBMED_12136144}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12136144 is the PubMed ID number.

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==About this Structure==

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[[Category: Paehler, A.]]

[[Category: Alpha betal]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ 2 22:59:56 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:41:04 2008''

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-[[Image:1kp0.jpg|left|200px]]
+{{Seed}}
+[[Image:1kp0.png|left|200px]]
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 {{STRUCTURE_1kp0|  PDB=1kp0  |  SCENE=  }}
-'''The Crystal Structure Analysis of Creatine Amidinohydrolase from Actinobacillus'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12136144}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12136144 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12136144}}
 ==About this Structure==
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 [[Category: Paehler, A.]]
 [[Category: Alpha betal]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:59:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:41:04 2008''