1tyg
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1tyg |SIZE=350|CAPTION= <scene name='initialview01'>1tyg</scene>, resolution 3.15Å | |PDB= 1tyg |SIZE=350|CAPTION= <scene name='initialview01'>1tyg</scene>, resolution 3.15Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= thiG,BSU11690 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= thiG,BSU11690 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tyg OCA], [http://www.ebi.ac.uk/pdbsum/1tyg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tyg RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Settembre, E C.]] | [[Category: Settembre, E C.]] | ||
[[Category: Zhai, H.]] | [[Category: Zhai, H.]] | ||
| - | [[Category: PO4]] | ||
[[Category: alpha beta barrel]] | [[Category: alpha beta barrel]] | ||
[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| Line 35: | Line 37: | ||
[[Category: these]] | [[Category: these]] | ||
| - | ''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 00:02:49 2008'' |
Revision as of 21:02, 30 March 2008
| |||||||
| , resolution 3.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | thiG,BSU11690 (Bacillus subtilis) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the thiazole synthase/ThiS complex
Overview
Thiazole synthase is the key enzyme involved in the formation of the thiazole moiety of thiamin pyrophosphate. We have determined the structure of this enzyme in complex with ThiS, the sulfur carrier protein, at 3.15 A resolution. Thiazole synthase is a tetramer with 222 symmetry. The monomer is a (betaalpha)(8) barrel with similarities to the aldolase class 1 and flavin mononucleotide dependent oxidoreductase and phosphate binding superfamilies. The sulfur carrier protein (ThiS) is a compact protein with a fold similar to that of ubiquitin. The structure allowed us to model the substrate, deoxy-D-xylulose 5-phosphate (DXP), in the active site. This model identified Glu98 and Asp182 as new active site residues likely to be involved in the catalysis of thiazole formation. The function of these residues was probed by mutagenesis experiments, which confirmed that both residues are essential for thiazole formation and identified Asp182 as the base involved in the deprotonation at C3 of the thiazole synthase DXP imine. Comparison of the ThiS binding surface to the surface of ubiquitin identified a conserved hydrophobic patch of unknown function on ubiquitin that may be involved in complex formation between ubiquitin and one of its binding partners.
About this Structure
1TYG is a Protein complex structure of sequences from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole synthase/sulfur carrier protein complex., Settembre EC, Dorrestein PC, Zhai H, Chatterjee A, McLafferty FW, Begley TP, Ealick SE, Biochemistry. 2004 Sep 21;43(37):11647-57. PMID:15362849
Page seeded by OCA on Mon Mar 31 00:02:49 2008
