2o6h
From Proteopedia
(New page: 200px<br /><applet load="2o6h" size="350" color="white" frame="true" align="right" spinBox="true" caption="2o6h, resolution 2.70Å" /> '''Lumazine synthase Ri...) |
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==Overview== | ==Overview== | ||
| - | 6,7-Dimethyl-8-ribityllumazine synthase (lumazine synthase; LS) catalyzes | + | 6,7-Dimethyl-8-ribityllumazine synthase (lumazine synthase; LS) catalyzes the penultimate step in the biosynthesis of riboflavin in plants and microorganisms. This protein is known to exhibit different quaternary assemblies between species, existing as free pentamers, decamers (dimers of pentamers) and icosahedrally arranged dodecamers of pentamers. A phylogenetic analysis on eubacterial, fungal and plant LSs allowed us to classify them into two categories: Type I LSs (pentameric or icosahedral) and Type II LSs (decameric). The Rhizobiales represent an order of alpha-proteobacteria that includes, among others, the genera Mesorhizobium, Agrobacterium and Brucella. Here, we present structural and kinetic studies on several LSs from Rhizobiales. Interestingly, Mesorhizobium and Brucella encode both a Type-I LS and a Type-II LS called RibH1 and RibH2, respectively. We show that Type II LSs appear to be almost inactive, whereas Type I LSs present a highly variable catalytic activity according to the genus. Additionally, we have solved four RibH1/RibH2 crystallographic structures from the genera Mesorhizobium and Brucella. The relationship between the active-site architecture and catalytic properties in these isoenzymes is discussed, and a model that describes the enzymatic behavior is proposed. Furthermore, sequence alignment studies allowed us to extend our results to the genus Agrobacterium. Our results suggest that the selective pressure controlling the riboflavin pathway favored the evolution of catalysts with low reaction rates, since the excess of flavins in the intracellular pool in Rhizobiales could act as a negative factor when these bacteria are exposed to oxidative or nitrosative stress. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Structural and | + | Structural and kinetic properties of lumazine synthase isoenzymes in the order Rhizobiales., Klinke S, Zylberman V, Bonomi HR, Haase I, Guimaraes BG, Braden BC, Bacher A, Fischer M, Goldbaum FA, J Mol Biol. 2007 Oct 26;373(3):664-80. Epub 2007 Aug 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17854827 17854827] |
[[Category: Brucella melitensis]] | [[Category: Brucella melitensis]] | ||
[[Category: Riboflavin synthase]] | [[Category: Riboflavin synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bacher, A.]] | [[Category: Bacher, A.]] | ||
| - | [[Category: Bonomi, H | + | [[Category: Bonomi, H R.]] |
| - | [[Category: Braden, B | + | [[Category: Braden, B C.]] |
[[Category: Fischer, M.]] | [[Category: Fischer, M.]] | ||
| - | [[Category: Goldbaum, F | + | [[Category: Goldbaum, F A.]] |
| - | [[Category: Guimaraes, B | + | [[Category: Guimaraes, B G.]] |
[[Category: Haase, I.]] | [[Category: Haase, I.]] | ||
[[Category: Klinke, S.]] | [[Category: Klinke, S.]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''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 18:15:00 2008'' |
Revision as of 16:15, 21 February 2008
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Lumazine synthase RibH1 from Brucella melitensis (Gene BMEI1187, Swiss-Prot entry Q8YGH2) complexed with inhibitor 5-Nitro-6-(D-Ribitylamino)-2,4(1H,3H) Pyrimidinedione
Overview
6,7-Dimethyl-8-ribityllumazine synthase (lumazine synthase; LS) catalyzes the penultimate step in the biosynthesis of riboflavin in plants and microorganisms. This protein is known to exhibit different quaternary assemblies between species, existing as free pentamers, decamers (dimers of pentamers) and icosahedrally arranged dodecamers of pentamers. A phylogenetic analysis on eubacterial, fungal and plant LSs allowed us to classify them into two categories: Type I LSs (pentameric or icosahedral) and Type II LSs (decameric). The Rhizobiales represent an order of alpha-proteobacteria that includes, among others, the genera Mesorhizobium, Agrobacterium and Brucella. Here, we present structural and kinetic studies on several LSs from Rhizobiales. Interestingly, Mesorhizobium and Brucella encode both a Type-I LS and a Type-II LS called RibH1 and RibH2, respectively. We show that Type II LSs appear to be almost inactive, whereas Type I LSs present a highly variable catalytic activity according to the genus. Additionally, we have solved four RibH1/RibH2 crystallographic structures from the genera Mesorhizobium and Brucella. The relationship between the active-site architecture and catalytic properties in these isoenzymes is discussed, and a model that describes the enzymatic behavior is proposed. Furthermore, sequence alignment studies allowed us to extend our results to the genus Agrobacterium. Our results suggest that the selective pressure controlling the riboflavin pathway favored the evolution of catalysts with low reaction rates, since the excess of flavins in the intracellular pool in Rhizobiales could act as a negative factor when these bacteria are exposed to oxidative or nitrosative stress.
About this Structure
2O6H is a Single protein structure of sequence from Brucella melitensis with and as ligands. Active as Riboflavin synthase, with EC number 2.5.1.9 Full crystallographic information is available from OCA.
Reference
Structural and kinetic properties of lumazine synthase isoenzymes in the order Rhizobiales., Klinke S, Zylberman V, Bonomi HR, Haase I, Guimaraes BG, Braden BC, Bacher A, Fischer M, Goldbaum FA, J Mol Biol. 2007 Oct 26;373(3):664-80. Epub 2007 Aug 21. PMID:17854827
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