1p74

<table><tr><td colspan='2'>[[1p74]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P74 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1P74 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;'>[[1p77|1p77]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AROE OR HI0655 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Shikimate_dehydrogenase Shikimate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.25 1.1.1.25] </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=1p74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p74 OCA], [http://pdbe.org/1p74 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p74 RCSB], [http://www.ebi.ac.uk/pdbsum/1p74 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p74 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Shikimate dehydrogenase catalyzes the NADPH-dependent reversible reduction of 3-dehydroshikimate to shikimate. We report the first X-ray structure of shikimate dehydrogenase from Haemophilus influenzae to 2.4-A resolution and its complex with NADPH to 1.95-A resolution. The molecule contains two domains, a catalytic domain with a novel open twisted alpha/beta motif and an NADPH binding domain with a typical Rossmann fold. The enzyme contains a unique glycine-rich P-loop with a conserved sequence motif, GAGGXX, that results in NADPH adopting a nonstandard binding mode with the nicotinamide and ribose moieties disordered in the binary complex. A deep pocket with a narrow entrance between the two domains, containing strictly conserved residues primarily contributed by the catalytic domain, is identified as a potential 3-dehydroshikimate binding pocket. The flexibility of the nicotinamide mononucleotide portion of NADPH may be necessary for the substrate 3-dehydroshikimate to enter the pocket and for the release of the product shikimate.

The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode.,Ye S, Von Delft F, Brooun A, Knuth MW, Swanson RV, McRee DE J Bacteriol. 2003 Jul;185(14):4144-51. PMID:12837789<ref>PMID:12837789</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 1p74" style="background-color:#fffaf0;"></div>

*[[Shikimate dehydrogenase|Shikimate dehydrogenase]]

[[Category: Bacterium influenzae lehmann and neumann 1896]]

[[Category: Brooun, A]]

[[Category: Delft, F von]]

[[Category: Knuth, M W]]

[[Category: McRee, D E]]

[[Category: Swanson, R V]]

[[Category: Ye, S]]

[[Category: Haemophilus influenzae]]

[[Category: Oxidoreductase]]