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3b1f
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| - | [[Image:3b1f.png|left|200px]] | ||
| - | < | + | ==Crystal structure of prephenate dehydrogenase from Streptococcus mutans== |
| - | + | <StructureSection load='3b1f' size='340' side='right'caption='[[3b1f]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3b1f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B1F FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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=3b1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b1f OCA], [https://pdbe.org/3b1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b1f RCSB], [https://www.ebi.ac.uk/pdbsum/3b1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b1f ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q8DUW0_STRMU Q8DUW0_STRMU] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Prephenate dehydrogenase (PDH) is a bacterial enzyme that catalyzes conversion of prephenate to 4-hydroxyphenylpyruvate through the oxidative decarboxylation pathway for tyrosine biosynthesis. This enzymatic pathway exists in prokaryotes but is absent in mammals, indicating that it is a potential target for the development of new antibiotics. The crystal structure of PDH from Streptococcus mutans in a complex with NAD(+) shows that the enzyme exists as a homo-dimer, each monomer consisting of two domains, a modified nucleotide binding N-terminal domain and a helical prephenate C-terminal binding domain. The latter is the dimerization domain. A structural comparison of PDHs from mesophilic S. mutans and thermophilic Aquifex aeolicus showed differences in the long loop between beta6 and beta7, which may be a reason for the high K(m) values of PDH from Streptococcus mutans. | ||
| - | + | Crystal structure of prephenate dehydrogenase from Streptococcus mutans.,Ku HK, Do NH, Song JS, Choi S, Yeon SH, Shin MH, Kim KJ, Park SR, Park IY, Kim SK, Lee SJ Int J Biol Macromol. 2011 Nov 1;49(4):761-6. Epub 2011 Jul 20. PMID:21798280<ref>PMID:21798280</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3b1f" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Large Structures]] |
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| - | == | + | |
| - | < | + | |
| - | [[Category: | + | |
[[Category: Streptococcus mutans]] | [[Category: Streptococcus mutans]] | ||
| - | [[Category: Choi | + | [[Category: Choi S]] |
| - | [[Category: Do | + | [[Category: Do NH]] |
| - | [[Category: Kim | + | [[Category: Kim KJ]] |
| - | [[Category: Ku | + | [[Category: Ku HK]] |
| - | [[Category: Lee | + | [[Category: Lee SJ]] |
| - | [[Category: Shin | + | [[Category: Shin MH]] |
| - | [[Category: Song | + | [[Category: Song JS]] |
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Current revision
Crystal structure of prephenate dehydrogenase from Streptococcus mutans
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Categories: Large Structures | Streptococcus mutans | Choi S | Do NH | Kim KJ | Ku HK | Lee SJ | Shin MH | Song JS
