| http://purl.uniprot.org/citations/27572957 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27572957 | http://www.w3.org/2000/01/rdf-schema#comment | "Trehalose serves as a key structural component in the cell wall of Mycobacterium tuberculosis. M. tuberculosis trehalose-6-phosphate phosphatase (MtbTPP), an essential enzyme in the trehalose biosynthesis OtsAB pathway, catalyzes the dephosphorylation of trehalose-6-phosphate (trehalose-6-P) to generate trehalose, and plays a critical role in M. tuberculosis survival-associated cell wall formation and permeability. Therefore, MtbTPP (OtsB2) is considered a promising potential target for discovery of antimicrobial drugs. However, the absence of structural information of MtbTPP restrains our understanding of its underlying catalytic mechanism. Here, we report the high-resolution crystal structures of apo active MtbTPP and its trehalose-6-P bound complex. The apo structure presents a canonical haloacid dehalogenase superfamily structural fold plus an extra N-terminal domain. The catalytic center is located in a positively charged cleft between the hydrolase domain and the cap domain, demonstrating a highly conserved substrate binding pocket. The role of residues interacting with the substrate in catalysis were probed by site-directed mutagenesis. Asp147, Asp149, Asp330, and Asp331 were found to be pivotal for the enzymatic activity of MtbTPP. The MtbTPP structures reported here provide insight into a key step in the biosynthesis of trehalose, which would facilitate future development of anti-TB therapeutics.-Shan, S., Min, H., Liu, T., Jiang, D., Rao, Z. Structural insight into dephosphorylation by trehalose 6-phosphate phosphatase (OtsB2) from Mycobacterium tuberculosis."xsd:string |
| http://purl.uniprot.org/citations/27572957 | http://purl.org/dc/terms/identifier | "doi:10.1096/fj.201600463r"xsd:string |
| http://purl.uniprot.org/citations/27572957 | http://purl.uniprot.org/core/author | "Liu T."xsd:string |
| http://purl.uniprot.org/citations/27572957 | http://purl.uniprot.org/core/author | "Rao Z."xsd:string |
| http://purl.uniprot.org/citations/27572957 | http://purl.uniprot.org/core/author | "Shan S."xsd:string |
| http://purl.uniprot.org/citations/27572957 | http://purl.uniprot.org/core/author | "Min H."xsd:string |
| http://purl.uniprot.org/citations/27572957 | http://purl.uniprot.org/core/author | "Jiang D."xsd:string |
| http://purl.uniprot.org/citations/27572957 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/27572957 | http://purl.uniprot.org/core/name | "FASEB J"xsd:string |
| http://purl.uniprot.org/citations/27572957 | http://purl.uniprot.org/core/pages | "3989-3996"xsd:string |
| http://purl.uniprot.org/citations/27572957 | http://purl.uniprot.org/core/title | "Structural insight into dephosphorylation by trehalose 6-phosphate phosphatase (OtsB2) from Mycobacterium tuberculosis."xsd:string |
| http://purl.uniprot.org/citations/27572957 | http://purl.uniprot.org/core/volume | "30"xsd:string |
| http://purl.uniprot.org/citations/27572957 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/27572957 |
| http://purl.uniprot.org/citations/27572957 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/27572957 |
| http://purl.uniprot.org/uniprot/#_P9WFZ5-mappedCitation-27572957 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/27572957 |
| http://purl.uniprot.org/uniprot/P9WFZ5 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/27572957 |