1rf5

<table><tr><td colspan='2'>[[1rf5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RF5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RF5 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rf4|1rf4]], [[1rf6|1rf6]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aroA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 "Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1rf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rf5 OCA], [http://pdbe.org/1rf5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rf5 RCSB], [http://www.ebi.ac.uk/pdbsum/1rf5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rf5 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:14763973</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1rf5" style="background-color:#fffaf0;"></div>

*[[EPSP synthase|EPSP synthase]]

[[Category: 3-phosphoshikimate 1-carboxyvinyltransferase]]

[[Category: Evans, J N]]

[[Category: Hilsenbeck, J L]]

[[Category: Kang, C]]

[[Category: Kim, H J]]

[[Category: Park, H]]

[[Category: Park, Y H]]

[[Category: Shuttleworth, W A]]

[[Category: Transferase]]