7cat

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[[Image:7cat.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_7cat| PDB=7cat | SCENE= }}
{{STRUCTURE_7cat| PDB=7cat | SCENE= }}
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'''THE NADPH BINDING SITE ON BEEF LIVER CATALASE'''
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===THE NADPH BINDING SITE ON BEEF LIVER CATALASE===
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==Overview==
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Beef liver and human erythrocyte catalases (EC 1.11.1.6) bind NADP tenaciously [Kirkman, H. N. &amp; 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.
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The line below this paragraph, {{ABSTRACT_PUBMED_3856839}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 3856839 is the PubMed ID number.
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{{ABSTRACT_PUBMED_3856839}}
==About this Structure==
==About this Structure==
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[[Category: Sicignano, A.]]
[[Category: Sicignano, A.]]
[[Category: Tanaka, N.]]
[[Category: Tanaka, N.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:44:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 14:30:38 2008''

Revision as of 11:30, 3 July 2008

Template:STRUCTURE 7cat

THE NADPH BINDING SITE ON BEEF LIVER CATALASE

Template:ABSTRACT PUBMED 3856839

About this Structure

7CAT is a Single protein structure. 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

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