1onl
From Proteopedia
(New page: 200px<br /><applet load="1onl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1onl, resolution 2.50Å" /> '''Crystal structure of...) |
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| - | [[Image:1onl.gif|left|200px]]<br /><applet load="1onl" size=" | + | [[Image:1onl.gif|left|200px]]<br /><applet load="1onl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1onl, resolution 2.50Å" /> | caption="1onl, resolution 2.50Å" /> | ||
'''Crystal structure of Thermus thermophilus HB8 H-protein of the glycine cleavage system'''<br /> | '''Crystal structure of Thermus thermophilus HB8 H-protein of the glycine cleavage system'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The glycine-cleavage system is a multi-enzyme complex consisting of four | + | The glycine-cleavage system is a multi-enzyme complex consisting of four different components (the P-, H-, T- and L-proteins). Recombinant H-protein corresponding to that from Thermus thermophilus HB8 has been overexpressed, purified and crystallized. Synchrotron radiation from BL44B2 at SPring-8 was used to collect a native data set to 2.5 A resolution. The crystals belonged to the hexagonal space group P6(5) and contained three molecules per asymmetric unit, with a solvent content of 39%. Because of the large number of molecules within a closely packed unit cell, this structure was solved by six-dimensional molecular replacement with the program EPMR using the pea H-protein structure as a search model and was refined to an R factor of 0.189 and a free R factor of 0.256. Comparison with the pea H-protein reveals two highly conserved regions surrounding the lipoyl-lysine arm. Both of these regions are negatively charged and each has additional properties that are conserved in H-proteins from many species, suggesting that these regions are involved in intermolecular interactions. One region has previously been proposed to constitute an interaction surface with T-protein, while the other may be involved in an interaction with P-protein. Meanwhile, the lipoyl-lysine arm of the T. thermophilus H-protein was found to be more flexible than that of the pea H-protein, supporting the hypothesis that H-protein does not form a stable complex with L-protein during the reaction. |
==About this Structure== | ==About this Structure== | ||
| - | 1ONL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http:// | + | 1ONL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ONL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Masui, R.]] | [[Category: Masui, R.]] | ||
[[Category: Nakai, T.]] | [[Category: Nakai, T.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: hybrid barrel-sandwich structure]] | [[Category: hybrid barrel-sandwich structure]] | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:46 2008'' |
Revision as of 12:19, 21 February 2008
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Crystal structure of Thermus thermophilus HB8 H-protein of the glycine cleavage system
Overview
The glycine-cleavage system is a multi-enzyme complex consisting of four different components (the P-, H-, T- and L-proteins). Recombinant H-protein corresponding to that from Thermus thermophilus HB8 has been overexpressed, purified and crystallized. Synchrotron radiation from BL44B2 at SPring-8 was used to collect a native data set to 2.5 A resolution. The crystals belonged to the hexagonal space group P6(5) and contained three molecules per asymmetric unit, with a solvent content of 39%. Because of the large number of molecules within a closely packed unit cell, this structure was solved by six-dimensional molecular replacement with the program EPMR using the pea H-protein structure as a search model and was refined to an R factor of 0.189 and a free R factor of 0.256. Comparison with the pea H-protein reveals two highly conserved regions surrounding the lipoyl-lysine arm. Both of these regions are negatively charged and each has additional properties that are conserved in H-proteins from many species, suggesting that these regions are involved in intermolecular interactions. One region has previously been proposed to constitute an interaction surface with T-protein, while the other may be involved in an interaction with P-protein. Meanwhile, the lipoyl-lysine arm of the T. thermophilus H-protein was found to be more flexible than that of the pea H-protein, supporting the hypothesis that H-protein does not form a stable complex with L-protein during the reaction.
About this Structure
1ONL is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Structure of Thermus thermophilus HB8 H-protein of the glycine-cleavage system, resolved by a six-dimensional molecular-replacement method., Nakai T, Ishijima J, Masui R, Kuramitsu S, Kamiya N, Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1610-8. Epub 2003, Aug 19. PMID:12925792
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