6jta | pdb_00006jta

Crystal Structure of D464A L465A mutant of FGAM Synthetase

spinqualitylabelsall models 6jta, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jta is a 1 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: ADP, EDO, GLN, GOL, MG, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PUR4_SALTY Publication Abstract from PubMed Transient tunnels that assemble and disassemble to facilitate passage of unstable intermediates in enzymes containing multiple reaction centers are controlled by allosteric cues. Using the 140-kDa purine biosynthetic enzyme PurL as a model system and a combination of biochemical and x-ray crystallographic studies, we show that long-distance communication between ~25-A distal active sites is initiated by an allosteric switch, residing in a conserved catalytic loop, adjacent to the synthetase active site. Further, combinatory experiments seeded from molecular dynamics simulations help to delineate transient states that bring out the central role of nonfunctional adaptor domains. We show that carefully orchestrated conformational changes, facilitated by interplay of dynamic interactions at the allosteric switch and adaptor-domain interface, control reactivity and concomitant formation of the ammonia tunnel. This study asserts that substrate channeling is modulated by allosteric hotspots that alter protein energy landscape, thereby allowing the protein to adopt transient conformations paramount to function. Role of allosteric switches and adaptor domains in long-distance cross-talk and transient tunnel formation.,Sharma N, Ahalawat N, Sandhu P, Strauss E, Mondal J, Anand R Sci Adv. 2020 Apr 3;6(14):eaay7919. doi: 10.1126/sciadv.aay7919. eCollection 2020, Apr. PMID:32284973 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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