4n02: Difference between revisions

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 <StructureSection load='4n02' size='340' side='right'caption='[[4n02]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4n02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N02 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4n02]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_CGSP14 Streptococcus pneumoniae CGSP14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N02 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FNR:1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-RIBITOL'>FNR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isopentenyl-diphosphate_Delta-isomerase Isopentenyl-diphosphate Delta-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.2 5.3.3.2] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FNR:1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-RIBITOL'>FNR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4n02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n02 OCA], [http://pdbe.org/4n02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n02 RCSB], [http://www.ebi.ac.uk/pdbsum/4n02 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n02 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4n02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n02 OCA], [https://pdbe.org/4n02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n02 RCSB], [https://www.ebi.ac.uk/pdbsum/4n02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n02 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/IDI2_STRPS IDI2_STRPS]] Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP) (By similarity).
+[https://www.uniprot.org/uniprot/IDI2_STRPS IDI2_STRPS] Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP) (By similarity).
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Isopentenyl diphosphate isomerase (IDI) is a key enzyme in the isoprenoid biosynthetic pathway and is required for all organisms that synthesize isoprenoid metabolites from mevalonate. Type 1 IDI (IDI-1) is a metalloprotein that is found in eukaryotes, whereas the type 2 isoform (IDI-2) is a flavoenzyme found in bacteria that is completely absent from human. IDI-2 from the pathogenic bacterium Streptococcus pneumoniae was recombinantly expressed in Escherichia coli. Steady-state kinetic studies of the enzyme indicated that FMNH2 (KM =0.3 muM) bound before isopentenyl diphosphate (KM =40 muM) in an ordered binding mechanism. An X-ray crystal structure at 1.4 A resolution was obtained for the holoenzyme in the closed conformation with a reduced flavin cofactor and two sulfate ions in the active site. These results helped to further approach the enzymatic mechanism of IDI-2 and, thus, open new possibilities for the rational design of antibacterial compounds against sequence-similar and structure-related pathogens such as Enterococcus faecalis or Staphylococcus aureus.
-Determination of Kinetics and the Crystal Structure of a Novel Type 2 Isopentenyl Diphosphate: Dimethylallyl Diphosphate Isomerase from Streptococcus pneumoniae.,de Ruyck J, Janczak MW, Neti SS, Rothman SC, Schubert HL, Cornish RM, Matagne A, Wouters J, Poulter CD Chembiochem. 2014 Jul 7;15(10):1452-8. doi: 10.1002/cbic.201402046. Epub 2014 Jun, 6. PMID:24910111<ref>PMID:24910111</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4n02" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Isopentenyl-diphosphate delta-isomerase|Isopentenyl-diphosphate delta-isomerase]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Isopentenyl-diphosphate Delta-isomerase]]
 [[Category: Large Structures]]
-[[Category: Streptococcus pneumoniae]]
+[[Category: Streptococcus pneumoniae CGSP14]]
-[[Category: Poulter, C D]]
+[[Category: Poulter CD]]
-[[Category: Ruyck, J de]]
+[[Category: Schubert HL]]
-[[Category: Schubert, H L]]
+[[Category: De Ruyck J]]
-[[Category: Isomerase]]
-[[Category: Tim barrel]]