1coz
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CTP:CYTIDINE-5'-TRIPHOSPHATE'>CTP</scene> | |LIGAND= <scene name='pdbligand=CTP:CYTIDINE-5'-TRIPHOSPHATE'>CTP</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Glycerol-3-phosphate_cytidylyltransferase Glycerol-3-phosphate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.39 2.7.7.39] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycerol-3-phosphate_cytidylyltransferase Glycerol-3-phosphate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.39 2.7.7.39] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1coz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1coz OCA], [http://www.ebi.ac.uk/pdbsum/1coz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1coz RCSB]</span> | ||
}} | }} | ||
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[[Category: Sanker, S.]] | [[Category: Sanker, S.]] | ||
[[Category: Weber, C H.]] | [[Category: Weber, C H.]] | ||
| - | [[Category: CTP]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:25:48 2008'' |
Revision as of 16:25, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | |||||||
| Activity: | Glycerol-3-phosphate cytidylyltransferase, with EC number 2.7.7.39 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CTP:GLYCEROL-3-PHOSPHATE CYTIDYLYLTRANSFERASE FROM BACILLUS SUBTILIS
Overview
BACKGROUND: The formation of critical intermediates in the biosynthesis of lipids and complex carbohydrates is carried out by cytidylyltransferases, which utilize CTP to form activated CDP-alcohols or CMP-acid sugars plus inorganic pyrophosphate. Several cytidylyltransferases are related and constitute a conserved family of enzymes. The eukaryotic members of the family are complex enzymes with multiple regulatory regions or repeated catalytic domains, whereas the bacterial enzyme, CTP:glycerol-3-phosphate cytidylyltransferase (GCT), contains only the catalytic domain. Thus, GCT provides an excellent model for the study of catalysis by the eukaryotic cytidylyltransferases. RESULTS: The crystal structure of GCT from Bacillus subtilis has been determined by multiwavelength anomalous diffraction using a mercury derivative and refined to 2.0 A resolution (R(factor) 0.196; R(free) 0.255). GCT is a homodimer; each monomer comprises an alpha/beta fold with a central 3-2-1-4-5 parallel beta sheet. Additional helices and loops extending from the alpha/beta core form a bowl that binds substrates. CTP, bound at each active site of the homodimer, interacts with the conserved (14)HXGH and (113)RTXGISTT motifs. The dimer interface incorporates part of a third motif, (63)RYVDEVI, and includes hydrophobic residues adjoining the HXGH sequence. CONCLUSIONS: Structure superpositions relate GCT to the catalytic domains from class I aminoacyl-tRNA synthetases, and thus expand the tRNA synthetase family of folds to include the catalytic domains of the family of cytidylyltransferases. GCT and aminoacyl-tRNA synthetases catalyze analogous reactions, bind nucleotides in similar U-shaped conformations, and depend on histidines from analogous HXGH motifs for activity. The structural and other similarities support proposals that GCT, like the synthetases, catalyzes nucleotidyl transfer by stabilizing a pentavalent transition state at the alpha-phosphate of CTP.
About this Structure
1COZ is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from bacillus subtilis., Weber CH, Park YS, Sanker S, Kent C, Ludwig ML, Structure. 1999 Sep 15;7(9):1113-24. PMID:10508782
Page seeded by OCA on Sun Mar 30 19:25:48 2008
