| http://purl.uniprot.org/citations/12837789 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12837789 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12837789 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/12837789 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.185.14.4144-4151.2003"xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.185.14.4144-4151.2003"xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.185.14.4144-4151.2003"xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/author | "Swanson R.V."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/author | "Swanson R.V."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/author | "Knuth M.W."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/author | "Knuth M.W."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/author | "Brooun A."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/author | "Brooun A."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/author | "Ye S."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/author | "Ye S."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/author | "McRee D.E."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/author | "McRee D.E."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/author | "Von Delft F."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/author | "Von Delft F."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/pages | "4144-4151"xsd:string |
| http://purl.uniprot.org/citations/12837789 | http://purl.uniprot.org/core/pages | "4144-4151"xsd:string |