2dzd: Difference between revisions

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New page: left|200px<br /><applet load="2dzd" size="350" color="white" frame="true" align="right" spinBox="true" caption="2dzd, resolution 2.4Å" /> '''Crystal structure of ...
 
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==Overview==
==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 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).


==About this Structure==
==About this Structure==
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[[Category: Pyruvate carboxylase]]
[[Category: Pyruvate carboxylase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Islam, M.N.]]
[[Category: Islam, M N.]]
[[Category: Kondo, H.]]
[[Category: Kondo, H.]]
[[Category: Kondo, S.]]
[[Category: Kondo, S.]]
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[[Category: pyruvate carboxylase]]
[[Category: pyruvate carboxylase]]


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