| http://purl.uniprot.org/citations/21185310 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21185310 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21185310 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/21185310 | http://www.w3.org/2000/01/rdf-schema#comment | "Enoyl-[acyl carrier protein] (ACP) reductase (ENR) is a key enzyme in type II fatty acid synthesis that catalyzes the last step in each elongation cycle. Therefore, it has been considered as a target for antibiotics. However, recent studies indicate that some pathogens have more than one ENR; in particular, Bacillus subtilis has two ENRs, FabI and FabL. The crystal structures of the ternary complexes of BsFaBI and BsFabL are found as a homotetramer showing the same overall structure despite a sequence identity of only 24%. The positions of the catalytic dyad of Tyr-(Xaa)(6)-Lys in FabL are almost identical to that of FabI, but a detailed structural analysis shows that FabL shares more structural similarities with FabG and other members of the SDR (short-chain alcohol dehydrogenase/reductase) family. The apo FabL structure shows significantly different conformations at the cofactor and the substrate-binding regions, and this resulted in a totally different tetrameric arrangement reflecting the flexibility of these regions in the absence of the cofactor and substrate/inhibitor."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2010.12.003"xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jmb.2010.12.003"xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/author | "Hong S.K."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/author | "Hong S.K."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/author | "Kim S.J."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/author | "Kim S.J."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/author | "Kim K.H."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/author | "Kim K.H."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/author | "Hwang K.Y."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/author | "Hwang K.Y."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/author | "Kim E.E."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/author | "Kim E.E."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/author | "Ha B.H."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/author | "Ha B.H."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/name | "J. Mol. Biol."xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/pages | "403-415"xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/pages | "403-415"xsd:string |
| http://purl.uniprot.org/citations/21185310 | http://purl.uniprot.org/core/title | "Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis."xsd:string |