1h0r

<table><tr><td colspan='2'>[[1h0r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. The April 2010 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Concanavalin A and Circular Permutation'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2010_4 10.2210/rcsb_pdb/mom_2010_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H0R FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FA1:2,3+-ANHYDRO-QUINIC+ACID'>FA1</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-dehydroquinate_dehydratase 3-dehydroquinate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.10 4.2.1.10] </span></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=1h0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h0r OCA], [http://pdbe.org/1h0r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h0r RCSB], [http://www.ebi.ac.uk/pdbsum/1h0r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h0r ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/AROQ_MYCTU AROQ_MYCTU]] Catalyzes a trans-dehydration via an enolate intermediate (By similarity).[HAMAP-Rule:MF_00169]

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== Publication Abstract from PubMed ==

The structures of enzymes catalyzing the reactions in central metabolic pathways are generally well conserved as are their catalytic mechanisms. The two types of 3-dehydroquinate dehydratase (DHQase) are therefore most unusual since they are unrelated at the sequence level and they utilize completely different mechanisms to catalyze the same overall reaction. The type I enzymes catalyze a cis-dehydration of 3-dehydroquinate via a covalent imine intermediate, while the type II enzymes catalyze a trans-dehydration via an enolate intermediate. Here we report the three-dimensional structures of a representative member of each type of biosynthetic DHQase. Both enzymes function as part of the shikimate pathway, which is essential in microorganisms and plants for the biosynthesis of aromatic compounds including folate, ubiquinone and the aromatic amino acids. An explanation for the presence of two different enzymes catalyzing the same reaction is presented. The absence of the shikimate pathway in animals makes it an attractive target for antimicrobial agents. The availability of these two structures opens the way for the design of highly specific enzyme inhibitors with potential importance as selective therapeutic agents.

The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction.,Gourley DG, Shrive AK, Polikarpov I, Krell T, Coggins JR, Hawkins AR, Isaacs NW, Sawyer L Nat Struct Biol. 1999 Jun;6(6):521-5. PMID:10360352<ref>PMID:10360352</ref>

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

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== References ==

<references/>

[[Category: 3-dehydroquinate dehydratase]]

[[Category: Myctu]]

[[Category: Abell, C]]

[[Category: Coggins, J R]]

[[Category: Frederickson, M]]

[[Category: Lapthorn, A J]]

[[Category: Robinson, D A]]

[[Category: Roszak, A W]]

[[Category: Shikimate pathway]]