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| - | [[Image:1onl.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1onl| PDB=1onl | SCENE= }} | | {{STRUCTURE_1onl| PDB=1onl | SCENE= }} |
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| - | '''Crystal structure of Thermus thermophilus HB8 H-protein of the glycine cleavage system'''
| + | ===Crystal structure of Thermus thermophilus HB8 H-protein of the glycine cleavage system=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12925792}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12925792 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12925792}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Rsgi]] | | [[Category: Rsgi]] |
| | [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:04:11 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:20:45 2008'' |
Revision as of 16:20, 27 July 2008
Template:STRUCTURE 1onl
Crystal structure of Thermus thermophilus HB8 H-protein of the glycine cleavage system
Template:ABSTRACT PUBMED 12925792
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
Page seeded by OCA on Sun Jul 27 19:20:45 2008
