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|8cat, resolution 2.50Å ()|
The NADPH binding site on beef liver catalase
Beef liver and human erythrocyte catalases (EC 18.104.22.168) bind NADP tenaciously [Kirkman, H. N. & Gaetani, G. F. (1984) Proc. Natl. Acad. Sci. USA 81, 4343-4348]. The position of NADP on beef liver catalase corresponds to the carboxyl-terminal polypeptide hinge in Penicillium vitale fungal catalase, which connects the common catalase structure to the additional flavodoxin-like domain. In contrast to nearly all other known structures of protein-bound NADP, NAD, and FAD, the NADP molecule of beef liver catalase is folded into a right-handed helix and bound, in part, in the vicinity of the carboxyl end of two alpha-helices. A water molecule (W7) occupies a pseudosubstrate site close to the C4 position of the nicotinamide and is hydrogen bonded to His-304. Although the NADP and heme groups approach each other to within 13.7 A, there is no direct interaction. The function of the NADP remains a mystery.
The NADPH binding site on beef liver catalase., Fita I, Rossmann MG, Proc Natl Acad Sci U S A. 1985 Mar;82(6):1604-8. PMID:3856839
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
8cat is a 2 chain structure with sequence from Bos taurus. This structure supersedes the now removed PDB entries and 1cat. The September 2004 RCSB PDB Molecule of the Month feature on Catalase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_9. Full crystallographic information is available from OCA.
- Fita I, Rossmann MG. The NADPH binding site on beef liver catalase. Proc Natl Acad Sci U S A. 1985 Mar;82(6):1604-8. PMID:3856839