Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate .cntdot. NADP+ ternary complex. substrate binding and a model for the transition state

Biochemistry ◽  
1990 ◽  
Vol 29 (13) ◽  
pp. 3263-3277 ◽  
Author(s):  
Christopher Bystroff ◽  
Stuart J. Oatley ◽  
Joseph Kraut
Keyword(s):  
Escherichia Coli ◽  
Transition State ◽  
Crystal Structures ◽  
Dihydrofolate Reductase ◽  
Ternary Complex ◽  
Substrate Binding

Light Activates Reduction of Methotrexate by NADPH in the Ternary Complex with Escherichia coli Dihydrofolate Reductase

1999 ◽  
Vol 69 (1) ◽  
pp. 77-85 ◽  
Author(s):  
Yong Qing Chen ◽  
Miriam Gulotta ◽  
H. T. Andrew Cheung ◽  
Robert Callender
Keyword(s):  
Escherichia Coli ◽  
Dihydrofolate Reductase ◽  
Ternary Complex

A study on the inhibition of dihydrofolate reductase (DHFR) from Escherichia coli by gold(i) phosphane compounds. X-ray crystal structures of (4,5-dichloro-1H-imidazolate-1-yl)-triphenylphosphane-gold(i) and (4,5-dicyano-1H-imidazolate-1-yl)-triphenylphosphane-gold(i)

2015 ◽  
Vol 44 (7) ◽  
pp. 3043-3056 ◽  
Author(s):  
Rossana Galassi ◽  
Camille Simon Oumarou ◽  
Alfredo Burini ◽  
Alessandro Dolmella ◽  
Daniela Micozzi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Crystal Structures ◽  
Dihydrofolate Reductase ◽  
X Ray

A study on the inhibition of dihydrofolate reductase (DHFR) by gold(i) compounds has been performed.

scholarly journals Refined crystal structures of Escherichia coli and chicken liver dihydrofolate reductase containing bound trimethoprim.

1985 ◽  
Vol 260 (1) ◽  
pp. 381-391 ◽  
Author(s):  
D A Matthews ◽  
J T Bolin ◽  
J M Burridge ◽  
D J Filman ◽  
K W Volz ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Crystal Structures ◽  
Dihydrofolate Reductase ◽  
Chicken Liver

Functional role of a mobile loop of Escherichia coli dihydrofolate reductase in transition-state stabilization

Biochemistry ◽  
1992 ◽  
Vol 31 (34) ◽  
pp. 7826-7833 ◽  
Author(s):  
Luyuan Li ◽  
Peter E. Wright ◽  
Stephen J. Benkovic ◽  
Christopher J. Falzone
Keyword(s):  
Escherichia Coli ◽  
Transition State ◽  
Dihydrofolate Reductase ◽  
Functional Role ◽  
Transition State Stabilization

scholarly journals Molecular mechanism for Rabex-5 GEF activation by Rabaptin-5

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Zhe Zhang ◽  
Tianlong Zhang ◽  
Shanshan Wang ◽  
Zhou Gong ◽  
Chun Tang ◽  
...  
Keyword(s):  
Binding Site ◽  
Crystal Structures ◽  
Molecular Mechanism ◽  
Ternary Complex ◽  
Substrate Binding ◽  
Unknown Mechanism ◽  
Substrate Binding Site ◽  
Biochemical Analyses ◽  
Α Helix

Rabex-5 and Rabaptin-5 function together to activate Rab5 and further promote early endosomal fusion in endocytosis. The Rabex-5 GEF activity is autoinhibited by the Rabex-5 CC domain (Rabex-5CC) and activated by the Rabaptin-5 C2-1 domain (Rabaptin-5C21) with yet unknown mechanism. We report here the crystal structures of Rabex-5 in complex with the dimeric Rabaptin-5C21 (Rabaptin-5C212) and in complex with Rabaptin-5C212 and Rab5, along with biophysical and biochemical analyses. We show that Rabex-5CC assumes an amphipathic α-helix which binds weakly to the substrate-binding site of the GEF domain, leading to weak autoinhibition of the GEF activity. Binding of Rabaptin-5C21 to Rabex-5 displaces Rabex-5CC to yield a largely exposed substrate-binding site, leading to release of the GEF activity. In the ternary complex the substrate-binding site of Rabex-5 is completely exposed to bind and activate Rab5. Our results reveal the molecular mechanism for the regulation of the Rabex-5 GEF activity.

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