Inferences about the catalytic domain of P-type ATPases from the tertiary structures of enzymes that catalyze the same elementary reaction

The machinery to catalyze elementary reactions is conserved, and the number of solved enzyme structures is increasing exponentially. Therefore, structures of enzymes that catalyze phosphate transfer are reviewed, and a supersecondary structure connecting the Walker A sequence to another sequence con...

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Bibliographic Details
Published in:FEBS Letters 1998-07, Vol.431 (3), p.309-314
Main Authors: Smirnova, Irina N, Kasho, Vladimir N, Faller, Larry D
Format: Article
Language:English
Subjects:
AAA family
ABC transporter
Active transport
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - metabolism
Adenosine Triphosphate - metabolism
Amino Acid Sequence
Animals
Binding Sites
Catalysis
Enzyme structure
Humans
Models, Chemical
Molecular Sequence Data
P-type pump
Phosphate transfer
Protein Structure, Tertiary
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Summary:The machinery to catalyze elementary reactions is conserved, and the number of solved enzyme structures is increasing exponentially. Therefore, structures of enzymes that catalyze phosphate transfer are reviewed, and a supersecondary structure connecting the Walker A sequence to another sequence containing functional amino acids is proposed as an additional signature for the active site. The new signature is used to infer the identity of the P-loop in P-type biological pumps and may be useful in predicting targets for site-directed mutagenesis in other enzymes of unknown structure like the AAA family and ABC transporters.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(98)00760-1