H
IPR035929

CoaB-like superfamily

InterPro entry
Short nameCoaB-like_sf
Overlapping entries
 

Description

CoaB adopts a 3-layer α/β/α fold with mixed β-sheets, which topologically resembles a combination of Rossmann-like and ribokinase-like folds. This structural domain can be found in human phosphopantothenoylcysteine (PPC) synthetase
[2]
and CoaB from the Escherichia coli coenzyme A bifunctional protein CoaBC
[1]
. The structure of these proteins predicts a ping pong mechanism with initial formation of an acyladenylate intermediate, followed by release of pyrophosphate and attack by cysteine to form the final products PPC and AMP.

References

1.Structural basis of CTP-dependent peptide bond formation in coenzyme A biosynthesis catalyzed by Escherichia coli PPC synthetase. Stanitzek S, Augustin MA, Huber R, Kupke T, Steinbacher S. Structure 12, 1977-88, (2004). View articlePMID: 15530362

2.Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution. Manoj N, Strauss E, Begley TP, Ealick SE. Structure 11, 927-36, (2003). View articlePMID: 12906824

Cross References

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