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1mc3
From Proteopedia
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[[Image:1mc3.jpg|left|200px]] | [[Image:1mc3.jpg|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF RFFH''' | '''CRYSTAL STRUCTURE OF RFFH''' | ||
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[[Category: Sauve, V.]] | [[Category: Sauve, V.]] | ||
[[Category: Sivaraman, J.]] | [[Category: Sivaraman, J.]] | ||
| - | [[Category: | + | [[Category: Bsgi]] |
| - | [[Category: | + | [[Category: Crystal structure]] |
| - | [[Category: | + | [[Category: Glucose-1-phosphate thymidylytransferase]] |
| - | [[Category: | + | [[Category: Montreal-kingston bacterial structural genomics initiative]] |
| - | [[Category: | + | [[Category: Rffh]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:52:34 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:52, 2 May 2008
CRYSTAL STRUCTURE OF RFFH
Overview
The enzyme glucose-1-phosphate thymidylyltransferase (RffH), the product of the rffh gene, catalyzes one of the steps in the synthesis of enterobacterial common antigen (ECA), a cell surface glycolipid found in Gram-negative enteric bacteria. In Escherichia coli two gene products, RffH and RmlA, catalyze the same enzymatic reaction and are homologous in sequence; however, they are part of different operons and function in different pathways. We report the crystal structure of RffH bound to deoxythymidine triphosphate (dTTP), the phosphate donor, and Mg(2+), refined at 2.6 A to an R-factor of 22.3% (R(free) = 28.4%). The crystal structure of RffH shows a tetrameric enzyme best described as a dimer of dimers. Each monomer has an overall alpha/beta fold and consists of two domains, a larger nucleotide binding domain (residues 1-115, 222-291) and a smaller sugar-binding domain (116-221), with the active site located at the domain interface. The Mg(2+) ion is coordinated by two conserved aspartates and the alpha-phosphate of deoxythymidine triphosphate. Its location corresponds well to that in a structurally similar domain of N-acetylglucosamine-1-phosphate uridylyltransferase (GlmU). Analysis of the RffH, RmlA, and GlmU complexes with substrates and products provides an explanation for their different affinities for Mg(2+) and leads to a proposal for the dynamics along the reaction pathway.
About this Structure
1MC3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of Escherichia coli glucose-1-phosphate thymidylyltransferase (RffH) complexed with dTTP and Mg2+., Sivaraman J, Sauve V, Matte A, Cygler M, J Biol Chem. 2002 Nov 15;277(46):44214-9. Epub 2002 Aug 8. PMID:12171937 Page seeded by OCA on Sat May 3 00:52:34 2008
Categories: Escherichia coli | Glucose-1-phosphate thymidylyltransferase | Single protein | BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative. | Cygler, M. | Matte, A. | Sauve, V. | Sivaraman, J. | Bsgi | Crystal structure | Glucose-1-phosphate thymidylytransferase | Montreal-kingston bacterial structural genomics initiative | Rffh | Structural genomic
