1rf5: Difference between revisions
New page: left|200px<br /><applet load="1rf5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rf5, resolution 2.3Å" /> '''Structural Studies of... |
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[[Image:1rf5.jpg|left|200px]]<br /><applet load="1rf5" size=" | [[Image:1rf5.jpg|left|200px]]<br /><applet load="1rf5" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1rf5, resolution 2.3Å" /> | caption="1rf5, resolution 2.3Å" /> | ||
'''Structural Studies of Streptococcus pneumoniae EPSP Synthase in Unliganded State'''<br /> | '''Structural Studies of Streptococcus pneumoniae EPSP Synthase in Unliganded State'''<br /> | ||
==Overview== | ==Overview== | ||
The shikimate pathway synthesizes aromatic amino acids and other essential | The shikimate pathway synthesizes aromatic amino acids and other essential metabolites that are necessary for bacteria, plants and fungi to survive. This pathway is not present in vertebrates and therefore represents an attractive target for antibacterial agents. We have successfully crystallized and solved the structure of unliganded, inhibitor-liganded and tetrahedral intermediate (TI)-liganded forms of Streptococcus pneumoniae EPSP synthase. The overall topology of the S. pneumoniae EPSP synthase is similar to that of the Escherichia coli EPSP synthase. In addition, the majority of residues responsible for ligand binding were conserved between the two proteins. TI-liganded structure provides absolute configuration of the C-2 atom from the F-PEP moiety of the enzyme-bound intermediate and also defines key residues responsible for the enzyme reaction. Comparison of the unliganded state and substrate-bound state of the enzyme provides insights into the structural mechanisms involved in dynamic events of ligand binding, domain movement and closure. This structural study of the pathogenic bacteria S. pneumoniae EPSP synthase with inhibitor and TI will provide invaluable information for the design of new-generation antibiotics. | ||
==About this Structure== | ==About this Structure== | ||
1RF5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Active as [http://en.wikipedia.org/wiki/3-phosphoshikimate_1-carboxyvinyltransferase 3-phosphoshikimate 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.19 2.5.1.19] Full crystallographic information is available from [http:// | 1RF5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Active as [http://en.wikipedia.org/wiki/3-phosphoshikimate_1-carboxyvinyltransferase 3-phosphoshikimate 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.19 2.5.1.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RF5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptococcus pneumoniae]] | [[Category: Streptococcus pneumoniae]] | ||
[[Category: Evans, J | [[Category: Evans, J N.]] | ||
[[Category: Hilsenbeck, J | [[Category: Hilsenbeck, J L.]] | ||
[[Category: Kang, C.]] | [[Category: Kang, C.]] | ||
[[Category: Kim, H | [[Category: Kim, H J.]] | ||
[[Category: Park, H.]] | [[Category: Park, H.]] | ||
[[Category: Park, Y | [[Category: Park, Y H.]] | ||
[[Category: Shuttleworth, W | [[Category: Shuttleworth, W A.]] | ||
[[Category: epsp synthase]] | [[Category: epsp synthase]] | ||
[[Category: glyphosate]] | [[Category: glyphosate]] | ||
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[[Category: shikimate pathway]] | [[Category: shikimate pathway]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:16 2008'' | ||
Revision as of 15:50, 21 February 2008
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Structural Studies of Streptococcus pneumoniae EPSP Synthase in Unliganded State
OverviewOverview
The shikimate pathway synthesizes aromatic amino acids and other essential metabolites that are necessary for bacteria, plants and fungi to survive. This pathway is not present in vertebrates and therefore represents an attractive target for antibacterial agents. We have successfully crystallized and solved the structure of unliganded, inhibitor-liganded and tetrahedral intermediate (TI)-liganded forms of Streptococcus pneumoniae EPSP synthase. The overall topology of the S. pneumoniae EPSP synthase is similar to that of the Escherichia coli EPSP synthase. In addition, the majority of residues responsible for ligand binding were conserved between the two proteins. TI-liganded structure provides absolute configuration of the C-2 atom from the F-PEP moiety of the enzyme-bound intermediate and also defines key residues responsible for the enzyme reaction. Comparison of the unliganded state and substrate-bound state of the enzyme provides insights into the structural mechanisms involved in dynamic events of ligand binding, domain movement and closure. This structural study of the pathogenic bacteria S. pneumoniae EPSP synthase with inhibitor and TI will provide invaluable information for the design of new-generation antibiotics.
About this StructureAbout this Structure
1RF5 is a Single protein structure of sequence from Streptococcus pneumoniae. Active as 3-phosphoshikimate 1-carboxyvinyltransferase, with EC number 2.5.1.19 Full crystallographic information is available from OCA.
ReferenceReference
Structural studies of Streptococcus pneumoniae EPSP synthase in unliganded state, tetrahedral intermediate-bound state and S3P-GLP-bound state., Park H, Hilsenbeck JL, Kim HJ, Shuttleworth WA, Park YH, Evans JN, Kang C, Mol Microbiol. 2004 Feb;51(4):963-71. PMID:14763973
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