2f59
From Proteopedia
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|PDB= 2f59 |SIZE=350|CAPTION= <scene name='initialview01'>2f59</scene>, resolution 2.30Å | |PDB= 2f59 |SIZE=350|CAPTION= <scene name='initialview01'>2f59</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= ribH1, ribH, ribH-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=235 Brucella abortus]) | |GENE= ribH1, ribH, ribH-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=235 Brucella abortus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1di0|1DI0]], [[1xn1|1XN1]], [[1t13|1T13]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f59 OCA], [http://www.ebi.ac.uk/pdbsum/2f59 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f59 RCSB]</span> | ||
}} | }} | ||
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[[Category: Klinke, S.]] | [[Category: Klinke, S.]] | ||
[[Category: Zylberman, V.]] | [[Category: Zylberman, V.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: INI]] | ||
[[Category: enzyme-substrate analogue]] | [[Category: enzyme-substrate analogue]] | ||
[[Category: inhibitor complex]] | [[Category: inhibitor complex]] | ||
[[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 Mon Mar 31 02:58:04 2008'' |
Revision as of 23:58, 30 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | ribH1, ribH, ribH-1 (Brucella abortus) | ||||||
| Activity: | Riboflavin synthase, with EC number 2.5.1.9 | ||||||
| Related: | 1DI0, 1XN1, 1T13
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Lumazine synthase RibH1 from Brucella abortus (Gene BruAb1_0785, Swiss-Prot entry Q57DY1) 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
2F59 is a Single protein structure of sequence from Brucella abortus. 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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