Conformational Change Rate-Limits GTP Hydrolysis:  The Mechanism of the ATP Sulfurylase−GTPase†

Biochemistry ◽  
1998 ◽  
Vol 37 (49) ◽  
pp. 17163-17169 ◽  
Author(s):  
Jiang Wei ◽  
Thomas S. Leyh
Keyword(s):  
Conformational Change ◽  
Atp Sulfurylase ◽  
Gtp Hydrolysis ◽  
Change Rate

Crystallographic studies of elongation factor G

1995 ◽  
Vol 73 (11-12) ◽  
pp. 1209-1216 ◽  
Author(s):  
Anders Liljas ◽  
Arnthor Ævarsson ◽  
Salam Al-Karadaghi ◽  
Maria Garber ◽  
Julia Zheltonosova ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Conformational Change ◽  
Conformational Changes ◽  
Elongation Factor ◽  
Elongation Factors ◽  
Elongation Factor G ◽  
Conformational States ◽  
Gtp Hydrolysis ◽  
Large Conformational Change ◽  
Factor G

The elongation factors G (EF-G) and Tu (EF-Tu) go through a number of conformation states in their functional cycles. Since they both are GTPases, have similar G domains and domains II, and have similar interactions with the nucleotides, then GTP hydrolysis must occur in similar ways. The crystal structures of two conformational states are known for EF-G and three are known for EF-Tu. The conformations of EF-G∙GDP and EF-Tu∙GTP are closely related. EF-Tu goes through a large conformational change upon GTP cleavage. This conformational change is to a large extent due to an altered interaction between the G domain and domains II and III. A number of kirromycin-resistant mutations are situated at the interface between domains I and III. The interface between the G domain and domain V in EF-G corresponds with this dynamic interface in EF-Tu. The contact area in EF-G is small and dominated by interactions between charged amino acids, which are part of a system that is observed to undergo conformational changes. Furthermore, a number of fusidic acid resistant mutants have been identified in this area. All of this evidence makes it likely that EF-G undergoes a large conformational change in its functional cycle. If the structures and conformational states of the elongation factors are related to a scheme in which the ribosome oscillates between two conformations, the pretranslocational and posttranslocational states, a model is arrived at in which EF-Tu drives the reaction in one direction and EF-G in the opposite. This may lead to the consequence that the GTP state of one factor is similar to the GDP state of the other. At the GTP hydrolysis state, the structures of the factors will be close to superimposable.Key words: elongation factor G, elongation factor Tu, crystal structures, conformational changes, ribosomal conformation.

n-Alkanols and halothane inhibit red cell anion transport and increase band 3 conformational change rate

Biochemistry ◽  
1985 ◽  
Vol 24 (18) ◽  
pp. 4859-4866 ◽  
Author(s):  
Stuart A. Forman ◽  
A. S. Verkman ◽  
James A. Dix ◽  
A. K. Solomon
Keyword(s):  
Conformational Change ◽  
Band 3 ◽  
Anion Transport ◽  
Red Cell ◽  
Change Rate

Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis

Nature ◽  
1990 ◽  
Vol 345 (6273) ◽  
pp. 309-315 ◽  
Author(s):  
Ilme Schlichting ◽  
Steven C. Almo ◽  
Gert Rapp ◽  
Keith Wilson ◽  
Kyriakos Petratos ◽  
...  
Keyword(s):  
Conformational Change ◽  
Gtp Hydrolysis ◽  
Time Resolved ◽  
P21 Protein ◽  
X Ray ◽  
Crystallographic Study ◽  
Ras P21

Structural basis for GTP hydrolysis and conformational change of MFN1 in mediating membrane fusion

2018 ◽  
Vol 25 (3) ◽  
pp. 233-243 ◽  
Author(s):  
Liming Yan ◽  
Yuanbo Qi ◽  
Xiaofang Huang ◽  
Caiting Yu ◽  
Lan Lan ◽  
...  
Keyword(s):  
Membrane Fusion ◽  
Conformational Change ◽  
Structural Basis ◽  
Gtp Hydrolysis

scholarly journals Uncoupling conformational change from GTP hydrolysis in a heterotrimeric G protein  -subunit

2004 ◽  
Vol 101 (20) ◽  
pp. 7560-7565 ◽  
Author(s):  
C. J. Thomas ◽  
X. Du ◽  
P. Li ◽  
Y. Wang ◽  
E. M. Ross ◽  
...  
Keyword(s):  
Conformational Change ◽  
G Protein ◽  
Protein Subunit ◽  
Gtp Hydrolysis ◽  
Heterotrimeric G Protein

scholarly journals GTP hydrolysis promotes disassembly of the atlastin crossover dimer during ER fusion

2018 ◽  
Vol 217 (12) ◽  
pp. 4184-4198 ◽  
Author(s):  
James Winsor ◽  
Ursula Machi ◽  
Qixiu Han ◽  
David D. Hackney ◽  
Tina H. Lee
Keyword(s):  
Membrane Fusion ◽  
Conformational Change ◽  
Initial Rate ◽  
Fusion Activity ◽  
Gtp Hydrolysis ◽  
Nucleotide Hydrolysis ◽  
Conformational Rearrangement ◽  
Gtp Binding ◽  
Over Time

Membrane fusion of the ER is catalyzed when atlastin GTPases anchored in opposing membranes dimerize and undergo a crossed over conformational rearrangement that draws the bilayers together. Previous studies have suggested that GTP hydrolysis triggers crossover dimerization, thus directly driving fusion. In this study, we make the surprising observations that WT atlastin undergoes crossover dimerization before hydrolyzing GTP and that nucleotide hydrolysis and Pi release coincide more closely with dimer disassembly. These findings suggest that GTP binding, rather than its hydrolysis, triggers crossover dimerization for fusion. In support, a new hydrolysis-deficient atlastin variant undergoes rapid GTP-dependent crossover dimerization and catalyzes fusion at an initial rate similar to WT atlastin. However, the variant cannot sustain fusion activity over time, implying a defect in subunit recycling. We suggest that GTP binding induces an atlastin conformational change that favors crossover dimerization for fusion and that the input of energy from nucleotide hydrolysis promotes complex disassembly for subunit recycling.

scholarly journals Evidence for conformational change-induced hydrolysis of β-tubulin-GTP

2020 ◽  
Author(s):  
Mohammadjavad Paydar ◽  
Benjamin H. Kwok
Keyword(s):  
Conformational Change ◽  
Intracellular Transport ◽  
Chemical Agent ◽  
Microtubule Depolymerization ◽  
Gtp Hydrolysis ◽  
Structural Framework ◽  
Microtubule Polymerization ◽  
Average Size ◽  
Cell Shape Formation ◽  
Β Tubulin

ABSTRACTMicrotubules, protein polymers of α/β-tubulin dimers, form the structural framework for many essential cellular processes including cell shape formation, intracellular transport, and segregation of chromosomes during cell division. It is known that tubulin-GTP hydrolysis is closely associated with microtubule polymerization dynamics. However, the precise roles of GTP hydrolysis in tubulin polymerization and microtubule depolymerization, and how it is initiated are still not clearly defined. We report here that tubulin-GTP hydrolysis can be triggered by conformational change induced by the depolymerizing kinesin-13 proteins or by the stabilizing chemical agent paclitaxel. We provide biochemical evidence that conformational change precedes tubulin-GTP hydrolysis, confirming this process is mechanically driven and structurally directional. Furthermore, we quantitatively measure the average size of the presumptive stabilizing “GTP cap” at growing microtubule ends. Together, our findings provide the molecular basis for tubulin-GTP hydrolysis and its role in microtubule polymerization and depolymerization.

scholarly journals A mutation uncouples the tubulin conformational and GTPase cycles, revealing allosteric control of microtubule dynamics

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Elisabeth A Geyer ◽  
Alexander Burns ◽  
Beth A Lalonde ◽  
Xuecheng Ye ◽  
Felipe-Andres Piedra ◽  
...  
Keyword(s):  
Conformational Change ◽  
Dynamic Instability ◽  
Dynamic Properties ◽  
Microtubule Dynamics ◽  
Gtpase Activity ◽  
Microtubule Dynamic ◽  
Gtp Hydrolysis ◽  
Allosteric Control

Microtubule dynamic instability depends on the GTPase activity of the polymerizing αβ-tubulin subunits, which cycle through at least three distinct conformations as they move into and out of microtubules. How this conformational cycle contributes to microtubule growing, shrinking, and switching remains unknown. Here, we report that a buried mutation in αβ-tubulin yields microtubules with dramatically reduced shrinking rate and catastrophe frequency. The mutation causes these effects by suppressing a conformational change that normally occurs in response to GTP hydrolysis in the lattice, without detectably changing the conformation of unpolymerized αβ-tubulin. Thus, the mutation weakens the coupling between the conformational and GTPase cycles of αβ-tubulin. By showing that the mutation predominantly affects post-GTPase conformational and dynamic properties of microtubules, our data reveal that the strength of the allosteric response to GDP in the lattice dictates the frequency of catastrophe and the severity of rapid shrinking.

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