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'''Structural Studies of Streptococcus pneumoniae EPSP Synthase in S3P-GLP Bound State''' | '''Structural Studies of Streptococcus pneumoniae EPSP Synthase in S3P-GLP Bound State''' | ||
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[[Category: Park, Y H.]] | [[Category: Park, Y H.]] | ||
[[Category: Shuttleworth, W A.]] | [[Category: Shuttleworth, W A.]] | ||
[[Category: | [[Category: Epsp synthase]] | ||
[[Category: | [[Category: Glyphosate]] | ||
[[Category: | [[Category: Pep]] | ||
[[Category: | [[Category: S. pneumoniae]] | ||
[[Category: | [[Category: S3p]] | ||
[[Category: | [[Category: Shikimate pathway]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:25:15 2008'' | |||
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Revision as of 07:25, 3 May 2008
Structural Studies of Streptococcus pneumoniae EPSP Synthase in S3P-GLP Bound 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
1RF6 is a Single protein structure of sequence from Streptococcus pneumoniae. 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 Page seeded by OCA on Sat May 3 07:25:15 2008