8cat
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(New page: 200px<br /> <applet load="8cat" size="450" color="white" frame="true" align="right" spinBox="true" caption="8cat, resolution 2.5Å" /> '''THE NADPH BINDING SI...)
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Revision as of 07:04, 18 November 2007
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THE NADPH BINDING SITE ON BEEF LIVER CATALASE
Overview
Beef liver and human erythrocyte catalases (EC 1.11.1.6) 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.
About this Structure
8CAT is a Single protein structure of sequence from Bos taurus with HEM and NDP as ligands. This structure superseeds the now removed PDB entries 3CAT and 1CAT. The following page contains interesting information on the relation of 8CAT with [Catalase]. Active as Catalase, with EC number 1.11.1.6 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Nov 18 09:11:32 2007
