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[[Image:7cat.gif|left|200px]] | [[Image:7cat.gif|left|200px]] | ||
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'''THE NADPH BINDING SITE ON BEEF LIVER CATALASE''' | '''THE NADPH BINDING SITE ON BEEF LIVER CATALASE''' | ||
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==About this Structure== | ==About this Structure== | ||
7CAT is a [[Single protein]] structure | 7CAT is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CAT OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Sicignano, A.]] | [[Category: Sicignano, A.]] | ||
[[Category: Tanaka, N.]] | [[Category: Tanaka, N.]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:44:11 2008'' | |||
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Revision as of 22:44, 4 May 2008
THE NADPH BINDING SITE ON BEEF LIVER CATALASE
OverviewOverview
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 StructureAbout this Structure
7CAT is a Single protein structure. Full crystallographic information is available from OCA.
ReferenceReference
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 May 4 22:44:11 2008