2obx
From Proteopedia
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- | [[Image:2obx.jpg|left|200px]] | + | [[Image:2obx.jpg|left|200px]] |
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- | '''Lumazine synthase RibH2 from Mesorhizobium loti (Gene mll7281, Swiss-Prot entry Q986N2) complexed with inhibitor 5-Nitro-6-(D-Ribitylamino)-2,4(1H,3H) Pyrimidinedione''' | + | {{Structure |
+ | |PDB= 2obx |SIZE=350|CAPTION= <scene name='initialview01'>2obx</scene>, resolution 2.53Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=INI:5-NITRO-6-RIBITYL-AMINO-2,4(1H,3H)-PYRIMIDINEDIONE'>INI</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Riboflavin_synthase Riboflavin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.9 2.5.1.9] | ||
+ | |GENE= ribH1, ribH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=381 Mesorhizobium loti]) | ||
+ | }} | ||
+ | |||
+ | '''Lumazine synthase RibH2 from Mesorhizobium loti (Gene mll7281, Swiss-Prot entry Q986N2) complexed with inhibitor 5-Nitro-6-(D-Ribitylamino)-2,4(1H,3H) Pyrimidinedione''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2OBX is a [ | + | 2OBX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mesorhizobium_loti Mesorhizobium loti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OBX OCA]. |
==Reference== | ==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:[http:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/17854827 17854827] |
[[Category: Mesorhizobium loti]] | [[Category: Mesorhizobium loti]] | ||
[[Category: Riboflavin synthase]] | [[Category: Riboflavin synthase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:57:43 2008'' |
Revision as of 15:57, 20 March 2008
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, resolution 2.53Å | |||||||
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Ligands: | and | ||||||
Gene: | ribH1, ribH (Mesorhizobium loti) | ||||||
Activity: | Riboflavin synthase, with EC number 2.5.1.9 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Lumazine synthase RibH2 from Mesorhizobium loti (Gene mll7281, Swiss-Prot entry Q986N2) 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
2OBX is a Single protein structure of sequence from Mesorhizobium loti. 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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