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Literature summary for 3.6.5.3 extracted from

  • Li, H.; Yao, X.Q.; Grant, B.J.
    Comparative structural dynamic analysis of GTPases (2018), PLoS Comput. Biol., 14, e1006364 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.5.3

Protein Variants

Protein Variants Comment Organism
additional information point mutations of the common key residues that are potentially important for mediating the inter-lobe communications can substantially disrupt the couplings around the nucleotide binding regions in EF-Tu Thermus aquaticus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Thermus aquaticus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Thermus aquaticus
-
 GDP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Thermus aquaticus Q01698
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
 Thermus aquaticus GDP + phosphate
-
 ?

Subunits

Subunits Comment Organism
More the enzyme contains a Ras-like domain, structure analysis and comparison, nucleotide-associated conformational dynamics, overview. Several common key residues are potentially important for mediating the inter-lobe communications Thermus aquaticus

Synonyms

Synonyms Comment Organism
EF-Tu
-
 Thermus aquaticus
elongation factor thermo unstable
-
 Thermus aquaticus

General Information

General Information Comment Organism
evolution there are three major GTPase superfamilies: small Ras-like GTPase, heterotrimeric G protein alphasubunit (Galpha) and protein-synthesizing GTPase. Underlying this functional difference are the low sequence identity (below 20%) and overall different molecular shapes among these three types of GTPases. In particular, whereas small G protein consists of a single canonical Ras-like catalytic domain (RasD), Galpha has an extra alpha-helical domain (HD) inserted and elongation factor EF-Tu has two extra beta-barrel domains (D2 and D3) subsequent to the C-terminus. In addition, Galpha can form a complex with Gbetagamma and undergoes a cycle of altered oligomeric states during function. In contrast to the functional and structural diversity, GTPases display significant conservation in the core structure of the catalytic domain. Small GTPase, Galpha, and EF-Tu contain a RasD consisting of six beta strands (beta1-beta6) and five alpha helices (alpha1-alpha5) flanking on both sides of the beta sheet. Three highly conserved loops named P-loop (PL), switch I (SI), and switch II (SII) constitute the primary sites coordinating the nucleotide phosphates. This structural similarity suggests that at a fundamental level small GTPase, Galpha, and EF-Tu may utilize the same mode of structural dynamics for their allosteric regulation, which is likely inherited from their common evolutionary ancestor. Structural comparison of Ras, Galphat and EF-Tu reveals common canonical Ras-like domain, nucleotide-associated conformational dynamics, molecular dynamics simulations, overview. Identification of EF-Tu specific key residues. But the enzymes show distinct nucleotide-associated flexibility and cross-correlation near functional regions, molecular dynamics simulations Thermus aquaticus
malfunction mutations of EF-Tu specific key residues significantly disrupt the couplings in EF-Tu Thermus aquaticus
physiological function the protein-synthesizing GTPases participate in initiation, elongation and termination of mRNA translation Thermus aquaticus