2dzd
From Proteopedia
(New page: 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 | + | 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 | + | [[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]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:04:17 2008'' |
Revision as of 15:04, 21 February 2008
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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).
About this Structure
2DZD is a Single protein structure of sequence from Geobacillus thermodenitrificans. Active as Pyruvate carboxylase, with EC number 6.4.1.1 Full crystallographic information is available from OCA.
Reference
Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans., Kondo S, Nakajima Y, Sugio S, Sueda S, Islam MN, Kondo H, Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):885-90. Epub 2007, Jul 17. PMID:17642515
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