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| | <StructureSection load='1onl' size='340' side='right'caption='[[1onl]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1onl' size='340' side='right'caption='[[1onl]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1onl]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ONL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ONL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1onl]] is a 3 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ONL FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GcvH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1onl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1onl OCA], [http://pdbe.org/1onl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1onl RCSB], [http://www.ebi.ac.uk/pdbsum/1onl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1onl ProSAT], [http://www.topsan.org/Proteins/RSGI/1onl TOPSAN]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1onl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1onl OCA], [https://pdbe.org/1onl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1onl RCSB], [https://www.ebi.ac.uk/pdbsum/1onl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1onl ProSAT], [https://www.topsan.org/Proteins/RSGI/1onl TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GCSH_THET8 GCSH_THET8]] The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity).[HAMAP-Rule:MF_00272] | + | [https://www.uniprot.org/uniprot/GCSH_THET8 GCSH_THET8] The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity).[HAMAP-Rule:MF_00272] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Flavobacterium thermophilum yoshida and oshima 1971]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ishijima, J]] | + | [[Category: Thermus thermophilus]] |
| - | [[Category: Kamiya, N]] | + | [[Category: Ishijima J]] |
| - | [[Category: Kuramitsu, S]] | + | [[Category: Kamiya N]] |
| - | [[Category: Masui, R]] | + | [[Category: Kuramitsu S]] |
| - | [[Category: Nakai, T]] | + | [[Category: Masui R]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Nakai T]] |
| - | [[Category: Hybrid barrel-sandwich structure]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| Structural highlights
Function
GCSH_THET8 The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity).[HAMAP-Rule:MF_00272]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nakai T, Ishijima J, Masui R, Kuramitsu S, Kamiya N. Structure of Thermus thermophilus HB8 H-protein of the glycine-cleavage system, resolved by a six-dimensional molecular-replacement method. Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1610-8. Epub 2003, Aug 19. PMID:12925792
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