Why was it necessary to use phosphoaminophosphohlc (ANP) in the ATP synthase enzyme active site rather than ATP to resolve the molecular structure of the ATP synthase active site by x-ray crystallography?

Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
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26
Why was it necessary to use
phosphoaminophosphonic
acid-adenylate ester
(ANP) in the ATP synthase enzyme active site rather than ATP to resolve the
molecular structure of the ATP synthase active site by x-ray crystallography?
ANP
Mg2+
E193
T164
x1
E189
B1
ATP cannot be used in a cell free system because it will be readily
Transcribed Image Text:Why was it necessary to use phosphoaminophosphonic acid-adenylate ester (ANP) in the ATP synthase enzyme active site rather than ATP to resolve the molecular structure of the ATP synthase active site by x-ray crystallography? ANP Mg2+ E193 T164 x1 E189 B1 ATP cannot be used in a cell free system because it will be readily
E193
T164
PET89
ATP cannot be used in a cell free system because it will be readily
hydrolyzed.
ANP has a S-S bond in the purine ring of the nucleotide to aid in
crystallography.
ATP is twice as large as ANP and will not fit in the ATP synthase active
site.
O
ANP is hydrophobic and ATP is hydrophilic, which makes ANP a better
reactant.
O
ANP is nonhydrolyzable and will trap the enzyme in the desired
conformation.
Transcribed Image Text:E193 T164 PET89 ATP cannot be used in a cell free system because it will be readily hydrolyzed. ANP has a S-S bond in the purine ring of the nucleotide to aid in crystallography. ATP is twice as large as ANP and will not fit in the ATP synthase active site. O ANP is hydrophobic and ATP is hydrophilic, which makes ANP a better reactant. O ANP is nonhydrolyzable and will trap the enzyme in the desired conformation.
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