3unw

Crystal Structure of Human GAC in Complex with Glutamate

spinqualitylabelsall models 3unw, resolution 2.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3unw is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GLU Related: 3uo9 Gene: GLS, GLS1, KIAA0838 (Homo sapiens) Activity: Glutaminase, with EC number 3.5.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum Function [GLSK_HUMAN] Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate in the brain. Isoform 2 lacks catalytic activity. Publication Abstract from PubMed Glutaminase (GLS1/2) catalyzes the conversion of l-glutamine to l-glutamate and ammonia. The level of a splice variant of GLS1 (GAC) is elevated in certain cancers, and GAC is specifically inhibited by bis-2-(5-phenylacetimido-1,2,4,thiadiazol-2-yl)ethyl sulfide (BPTES). We report here the first full-length crystal structure of GAC in the presence and absence of BPTES molecules. Two BPTES molecules bind at an interface region of the GAC tetramer in a manner that appears to lock the GAC tetramer into a nonproductive conformation. The importance of these loops with regard to overall enzymatic activity of the tetramer was revealed by a series of GAC point mutants designed to create a BPTES resistant GAC. Full-Length Human Glutaminase in Complex with an Allosteric Inhibitor.,Delabarre B, Gross S, Fang C, Gao Y, Jha A, Jiang F, Song J J, Wei W, Hurov JB Biochemistry. 2011 Nov 18. PMID:22049910 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glutaminase

Proteopedia Page Contributors and Editors (what is this?)

OCA