| http://purl.uniprot.org/citations/30576731 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/30576731 | http://www.w3.org/2000/01/rdf-schema#comment | "The Mycobacterium tuberculosis (Mtb) Rv2747 gene encodes for a functional protein known as ArgA, which plays an important role in the first step of the l-arginine biosynthesis pathway. ArgA transfers the acetyl group from the acetyl-CoA to either l-glutamate or l-glutamine, which are the known substrates. Here, we present two crystal structures of ArgA: one complexed with CoA and product bound N-acetylglutamine and the other complexed with acetyl-CoA and the inhibitor l-arginine at 2.3 and 3.0 Å resolution respectively. The Mtb ArgA protomer was found to have a "V" cleft and a "β" bulge, archetypal of a classical GCN5-related N-acetyltransferase superfamily of proteins. The product bound form implies that ArgA can also acetylate l-glutamine like l-glutamate. The active site is strongly inhibited by l-arginine resulting in a closed conformation of ArgA and both l-arginine and N-acetylglutamine were found to occupy at the same active site. Together with structural analysis, molecular docking studies, microscale thermophoresis and enzyme inhibition assays, we conclude that l-glutamine, l-glutamate and l-arginine, all occupy at the same active site of ArgA. Furthermore in case of Mtb ArgA, l-arginine does not act as an allosteric inhibitor unlike other N-acetylglutamate synthase family of proteins."xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.ijbiomac.2018.12.163"xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/author | "Kumar S."xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/author | "Srinivasan A."xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/author | "Gourinath S."xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/author | "Menon S."xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/author | "Das U."xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/author | "Pal R.K."xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/author | "Vijayan R."xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/author | "Dharavath S."xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/author | "Singh E."xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/author | "Tiruttani Subhramanyam U.K."xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/date | "2019"xsd:gYear |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/name | "Int J Biol Macromol"xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/pages | "970-978"xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/title | "Structural insights into the substrate binding mechanism of novel ArgA from Mycobacterium tuberculosis."xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://purl.uniprot.org/core/volume | "125"xsd:string |
| http://purl.uniprot.org/citations/30576731 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/30576731 |
| http://purl.uniprot.org/citations/30576731 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/30576731 |
| http://purl.uniprot.org/uniprot/#_O33289-mappedCitation-30576731 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/30576731 |
| http://purl.uniprot.org/uniprot/O33289 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/30576731 |