1g4e
From Proteopedia
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- | [[Image:1g4e.jpg|left|200px]] | + | [[Image:1g4e.jpg|left|200px]] |
- | + | ||
- | '''THIAMIN PHOSPHATE SYNTHASE''' | + | {{Structure |
+ | |PDB= 1g4e |SIZE=350|CAPTION= <scene name='initialview01'>1g4e</scene>, resolution 1.60Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Thiamine-phosphate_diphosphorylase Thiamine-phosphate diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.3 2.5.1.3] | ||
+ | |GENE= THIC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
+ | }} | ||
+ | |||
+ | '''THIAMIN PHOSPHATE SYNTHASE''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1G4E is a [ | + | 1G4E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G4E OCA]. |
==Reference== | ==Reference== | ||
- | Structural characterization of the enzyme-substrate, enzyme-intermediate, and enzyme-product complexes of thiamin phosphate synthase., Peapus DH, Chiu HJ, Campobasso N, Reddick JJ, Begley TP, Ealick SE, Biochemistry. 2001 Aug 28;40(34):10103-14. PMID:[http:// | + | Structural characterization of the enzyme-substrate, enzyme-intermediate, and enzyme-product complexes of thiamin phosphate synthase., Peapus DH, Chiu HJ, Campobasso N, Reddick JJ, Begley TP, Ealick SE, Biochemistry. 2001 Aug 28;40(34):10103-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11513589 11513589] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
- | ''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 11:18:04 2008'' |
Revision as of 09:18, 20 March 2008
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, resolution 1.60Å | |||||||
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Gene: | THIC (Bacillus subtilis) | ||||||
Activity: | Thiamine-phosphate diphosphorylase, with EC number 2.5.1.3 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
THIAMIN PHOSPHATE SYNTHASE
Overview
Thiamin phosphate synthase catalyzes the formation of thiamin phosphate from 4-amino-5-(hydroxymethyl)-2-methylpyrimidine pyrophosphate and 5-(hydroxyethyl)-4-methylthiazole phosphate. Several lines of evidence suggest that the reaction proceeds via a dissociative mechanism. The previously determined crystal structure of thiamin phosphate synthase in complex with the reaction products, thiamin phosphate and magnesium pyrophosphate, provided a view of the active site and suggested a number of additional experiments. We report here seven new crystal structures primarily involving crystals of S130A thiamin phosphate synthase soaked in solutions containing substrates or products. We prepared S130A thiamin phosphate synthase with the intent of characterizing the enzyme-substrate complex. Surprisingly, in three thiamin phosphate synthase structures, the active site density cannot be modeled as either substrates or products. For these structures, the best fit to the electron density is provided by a model that consists of independent pyrimidine, pyrophosphate, and thiazole phosphate fragments, consistent with a carbenium ion intermediate. The resulting carbenium ion is likely to be further stabilized by proton transfer from the pyrimidine amino group to the pyrophosphate to give the pyrimidine iminemethide, which we believe is the species that is observed in the crystal structures.
About this Structure
1G4E is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Structural characterization of the enzyme-substrate, enzyme-intermediate, and enzyme-product complexes of thiamin phosphate synthase., Peapus DH, Chiu HJ, Campobasso N, Reddick JJ, Begley TP, Ealick SE, Biochemistry. 2001 Aug 28;40(34):10103-14. PMID:11513589
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