Structural highlights
3q6j is a 2 chain structure with sequence from Xanthobacter autotrophicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , , , , |
| Related: | 2c3d, 1mo9, 1mok |
| Activity: | 2-oxopropyl-CoM reductase (carboxylating), with EC number 1.8.1.5 |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Publication Abstract from PubMed
The structure of 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) has been determined in a state in which CO(2) is observed providing insights into the mechanism of carboxylation. In the substrate encapsulated state of the enzyme, CO(2) is bound at the base of a narrow hydrophobic substrate access channel. The base of the channel is demarcated by a transition from a hydrophobic to hydrophilic environment where CO(2) is located in position for attack on the carbanion of the ketopropyl group of the substrate to ultimately produce acetoacetate. This binding mode effectively discriminates against H(2)O and prevents protonation of the ketopropyl leaving group. STRUCTURED SUMMARY: 2-KPCCbinds to 2-KPCC by x-ray crystallography (View interaction).
Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase.,Pandey AS, Mulder DW, Ensign SA, Peters JW FEBS Lett. 2011 Feb 4;585(3):459-64. Epub 2010 Dec 27. PMID:21192936[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pandey AS, Mulder DW, Ensign SA, Peters JW. Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase. FEBS Lett. 2011 Feb 4;585(3):459-64. Epub 2010 Dec 27. PMID:21192936 doi:10.1016/j.febslet.2010.12.035
