2dzd: Difference between revisions

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[[Image:2dzd.~~jpg~~|left|200px]]

[[Image:2dzd.png|left|200px]]

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~~'''~~Crystal structure of the biotin carboxylase domain of pyruvate carboxylase~~'''~~

===Crystal structure of the biotin carboxylase domain of pyruvate carboxylase===

~~==Overview==~~

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The ~~biotin carboxylase (BC) domain of pyruvate carboxylase (PC) from Bacillus thermodenitrificans (BC-bPC) was crystallized in an orthorhombic form (space group P2(1)2(1)2(1))~~, ~~with unit-cell parameters a = 79.6~~, ~~b = 116.0, c = 115.7 A. Two BC protomers are contained in~~ the ~~asymmetric unit. Diffraction data were collected~~ at ~~100 K and the crystal structure was solved by the molecular-replacement method and refined against reflections in the 20~~.~~0-2~~.~~4 A resolution range~~, ~~giving an R factor of 0.235 and a free R factor of 0.292. The overall structure of BC-bPC~~ is ~~similar to those of~~ the ~~BC subunits of Aquifex aeolicus PC (BC-aPC) and Escherichia coli ACC (BC-eACC)~~. ~~The crystal structure revealed that BC~~-~~bPC forms a unique dimeric quaternary structure, which might be caused as a result of the division of the BC domain from the rest of the protein. The position of domain B in BC~~-~~bPC differs from those in other enzymes of similar structure (BC-aPC and BC-eACC).~~

The line below this paragraph, {{ABSTRACT_PUBMED_17642515}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17642515 is the PubMed ID number.

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==About this Structure==

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[[Category: Ligase]]

[[Category: Pyruvate carboxylase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 01~~:39:13 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:00:54 2008''

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-[[Image:2dzd.jpg|left|200px]]
+{{Seed}}
+[[Image:2dzd.png|left|200px]]
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 {{STRUCTURE_2dzd|  PDB=2dzd  |  SCENE=  }}
-'''Crystal structure of the biotin carboxylase domain of pyruvate carboxylase'''
+===Crystal structure of the biotin carboxylase domain of pyruvate carboxylase===
-==Overview==
+<!--
-The biotin carboxylase (BC) domain of pyruvate carboxylase (PC) from Bacillus thermodenitrificans (BC-bPC) was crystallized in an orthorhombic form (space group P2(1)2(1)2(1)), with unit-cell parameters a = 79.6, b = 116.0, c = 115.7 A. Two BC protomers are contained in the asymmetric unit. Diffraction data were collected at 100 K and the crystal structure was solved by the molecular-replacement method and refined against reflections in the 20.0-2.4 A resolution range, giving an R factor of 0.235 and a free R factor of 0.292. The overall structure of BC-bPC is similar to those of the BC subunits of Aquifex aeolicus PC (BC-aPC) and Escherichia coli ACC (BC-eACC). The crystal structure revealed that BC-bPC forms a unique dimeric quaternary structure, which might be caused as a result of the division of the BC domain from the rest of the protein. The position of domain B in BC-bPC differs from those in other enzymes of similar structure (BC-aPC and BC-eACC).
+The line below this paragraph, {{ABSTRACT_PUBMED_17642515}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17642515 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17642515}}
 ==About this Structure==
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 [[Category: Ligase]]
 [[Category: Pyruvate carboxylase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 01:39:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:00:54 2008''