2ate | pdb_00002ate
Structure of the complex of PurE with NitroAIR
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| 2ate, resolution 1.80Å | |||||||||||||
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| Ligands: | MSE, NIA | ||||||||||||
| Gene: | purE (Escherichia coli) | ||||||||||||
| Activity: | Phosphoribosylaminoimidazole carboxylase, with EC number 4.1.1.21 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
Structural studies, sequence alignments, and biochemistry have provided new insights into the evolution of the purine biosynthetic pathway. The importance of chemistry, the binding of ribose 5-phosphate (common to all purine biosynthetic intermediates), and transient protein-protein interactions in channeling of chemically unstable intermediates have all been examined in the past few years.
About this Structure
2ATE is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Modular evolution of the purine biosynthetic pathway., Kappock TJ, Ealick SE, Stubbe J, Curr Opin Chem Biol. 2000 Oct;4(5):567-72. PMID:11006546
Page seeded by OCA on Mon Mar 31 01:57:02 2008
