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| - | [[Image:1coz.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1coz| PDB=1coz | SCENE= }} | | {{STRUCTURE_1coz| PDB=1coz | SCENE= }} |
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| - | '''CTP:GLYCEROL-3-PHOSPHATE CYTIDYLYLTRANSFERASE FROM BACILLUS SUBTILIS'''
| + | ===CTP:GLYCEROL-3-PHOSPHATE CYTIDYLYLTRANSFERASE FROM BACILLUS SUBTILIS=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10508782}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10508782 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10508782}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Weber, C H.]] | | [[Category: Weber, C H.]] |
| | [[Category: Transferase]] | | [[Category: Transferase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:57:45 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:02:37 2008'' |
Revision as of 18:02, 30 June 2008
Template:STRUCTURE 1coz
CTP:GLYCEROL-3-PHOSPHATE CYTIDYLYLTRANSFERASE FROM BACILLUS SUBTILIS
Template:ABSTRACT PUBMED 10508782
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 Mon Jun 30 21:02:37 2008
