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| | <StructureSection load='1p77' size='340' side='right'caption='[[1p77]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='1p77' size='340' side='right'caption='[[1p77]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1p77]] is a 1 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=1P77 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1P77 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1p77]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P77 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ATR:2-MONOPHOSPHOADENOSINE-5-DIPHOSPHATE'>ATR</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]] 1.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1p74|1p74]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ATR:2-MONOPHOSPHOADENOSINE-5-DIPHOSPHATE'>ATR</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p77 OCA], [https://pdbe.org/1p77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p77 RCSB], [https://www.ebi.ac.uk/pdbsum/1p77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p77 ProSAT]</span></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=1p77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p77 OCA], [http://pdbe.org/1p77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p77 RCSB], [http://www.ebi.ac.uk/pdbsum/1p77 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p77 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AROE_HAEIN AROE_HAEIN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Shikimate dehydrogenase|Shikimate dehydrogenase]] | + | *[[Shikimate dehydrogenase 3D structures|Shikimate dehydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium influenzae lehmann and neumann 1896]] | |
| - | [[Category: Large Structures]] | |
| - | [[Category: Shikimate dehydrogenase]] | |
| - | [[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: Haemophilus influenzae]] |
| - | [[Category: Nadph]] | + | [[Category: Large Structures]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Brooun A]] |
| | + | [[Category: Knuth MW]] |
| | + | [[Category: McRee DE]] |
| | + | [[Category: Swanson RV]] |
| | + | [[Category: Ye S]] |
| | + | [[Category: Von Delft F]] |
| Structural highlights
Function
AROE_HAEIN
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ye S, Von Delft F, Brooun A, Knuth MW, Swanson RV, McRee DE. The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode. J Bacteriol. 2003 Jul;185(14):4144-51. PMID:12837789
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