Sandbox Reserved 1580
From Proteopedia
(Difference between revisions)
Line 5: | Line 5: | ||
== Overview == | == Overview == | ||
- | Glutaminyl-tRNA synthetase or GlnRS is a class 1 tRNA synthetase that requires tRNA binding for adenylate synthesis, which suggests that the large substrate could be required to form the active site structure. <ref name=frank>12737824</ref> Genetic evidence shows that induced fit conformational changes are a big part in the mechanism of GlnRS. <ref name=frank>12737824</ref> Glutaminyl-tRNA synthetase is an enzyme who's function is to catalyze the transfer of the amino acid glutamine to the A76 hydroxyl group of tRNA^Gln. <ref name=frank | + | Glutaminyl-tRNA synthetase or GlnRS is a class 1 tRNA synthetase that requires tRNA binding for adenylate synthesis, which suggests that the large substrate could be required to form the active site structure. <ref name=frank>12737824</ref> Genetic evidence shows that induced fit conformational changes are a big part in the mechanism of GlnRS. <ref name=frank>PMID:12737824</ref> Glutaminyl-tRNA synthetase is an enzyme who's function is to catalyze the transfer of the amino acid glutamine to the A76 hydroxyl group of tRNA^Gln. <ref name=frank /> Glutaminyl-tRNA synthetase was highly expressed in the developing of unborn-baby related, human brains in many cell types. <ref name=Atrophy>PMID:24656866</ref> |
== Structure == | == Structure == | ||
- | The crystal structure of ligand-free E. coli glutaminyl-tRNA synthetase at 2.4 A shows substrate binding is needed to construct a catalytically proficient active site. <ref name=frank | + | The crystal structure of ligand-free E. coli glutaminyl-tRNA synthetase at 2.4 A shows substrate binding is needed to construct a catalytically proficient active site. <ref name=frank /> Five hundred and twenty-one of the five hundred and thirty-three amino acids were able to be built into the electron density maps. <ref name=frank /> The backbone atoms of 94 amino acid residues, <scene name='82/824625/Backbone_atoms_amino_acid_comp/1'>25–31, 36–63, 77–99, 213–239, and 252–260</scene> could be superimposed on their counterparts showing similarities close to each other. <ref name=frank /> When superimposed there were few differences the unligand enzyme and the tRNA-bound enzyme.<ref name=frank /> One of the amino acids in the <scene name='82/824625/Loop_compromising_amino_acids/1'>surface loop compromising amino acids 64-76</scene> of the dinucleotide fold adopts a new arrangement in the unligand enzyme. <ref name=frank /> Also, two amino acids in different surface loops in C-terminal beta barrel regions are fully disordered, just like the surface loop compromising amino acids. <ref name=frank /> |
== Mutations == | == Mutations == | ||
- | Mutations in the coding of glutaminyl-tRNA synthetase can cause seizures especially in infants. <ref name=Atrophy | + | Mutations in the coding of glutaminyl-tRNA synthetase can cause seizures especially in infants. <ref name=Atrophy /> The mutations in the coding can cause progressive microcephaly and the tissue of the brain to waste away in several different regions including the cerebellar vermis, cerebral cortex, and the cerebellar hemispheres. <ref name=Atrophy /> Progressive microcephaly is a condition that involves mutations in gene coding of brain survival. <ref name=Atrophy /> Seizures are severe but not very common compared to the other disorders. <ref name=Atrophy /> Glutaminyl-tRNA synthetase is important during the brain development stages. <ref name=Atrophy /> The cerebral cortex and the cerebellar vermis are the primarly affected areas with a mutation in the coding of glutaminyl-tRNA synthetase and is a big distinction between it and other coding mutations, for example PCH, which is a caused by mutations but with it the cerebellum and the brain stem are mostly affected. <ref name=Atrophy /> |
Revision as of 17:33, 2 December 2019
This Sandbox is Reserved from September 14, 2021, through May 31, 2022, for use in the class Introduction to Biochemistry taught by User:John Means at the University of Rio Grande, Rio Grande, OH, USA. This reservation includes 5 reserved sandboxes (Sandbox Reserved 1590 through Sandbox Reserved 1594). |
To get started:
More help: Help:Editing. For an example of a student Proteopedia page, please see Photosystem II, Tetanospasmin, or Guanine riboswitch. |
Glutaminyl-tRNA Synthetase
|
References
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 12737824
- ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 Zhang X, Ling J, Barcia G, Jing L, Wu J, Barry BJ, Mochida GH, Hill RS, Weimer JM, Stein Q, Poduri A, Partlow JN, Ville D, Dulac O, Yu TW, Lam AT, Servattalab S, Rodriguez J, Boddaert N, Munnich A, Colleaux L, Zon LI, Soll D, Walsh CA, Nabbout R. Mutations in QARS, encoding glutaminyl-tRNA synthetase, cause progressive microcephaly, cerebral-cerebellar atrophy, and intractable seizures. Am J Hum Genet. 2014 Apr 3;94(4):547-58. doi: 10.1016/j.ajhg.2014.03.003. Epub, 2014 Mar 20. PMID:24656866 doi:http://dx.doi.org/10.1016/j.ajhg.2014.03.003