2npx: Difference between revisions
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[[Image:2npx.jpg|left|200px]]<br /><applet load="2npx" size=" | [[Image:2npx.jpg|left|200px]]<br /><applet load="2npx" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2npx, resolution 2.4Å" /> | caption="2npx, resolution 2.4Å" /> | ||
'''NADH BINDING SITE AND CATALYSIS OF NADH PEROXIDASE'''<br /> | '''NADH BINDING SITE AND CATALYSIS OF NADH PEROXIDASE'''<br /> | ||
==Overview== | ==Overview== | ||
The structure of the complex between cofactor NADH and the enzyme NADH | The structure of the complex between cofactor NADH and the enzyme NADH peroxidase from Streptococcus faecalis 10C1 (Enterococcus faecalis) has been determined by crystal soaking, X-ray data collection, model building of NADH and refinement at 0.24-nm resolution based on the known enzyme structure [Stehle, T., Ahmed, S. A., Claiborne, A. & Schulz, G. E. (1991) J. Mol. Biol. 221, 1325-1344]. Apart from NADH, the catalytic center of the enzyme contains FAD and a cysteine that shuttles between thiolate and sulfenic acid states. Unfortunately, this cysteine was irreversibly oxidized to a cysteine sulfonic acid in the established enzyme structure. Based on the geometry of the catalytic center, we discuss the stabilization of the oxidation-sensitive sulfenic acid and propose a reaction mechanism. | ||
==About this Structure== | ==About this Structure== | ||
2NPX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with CYO, FAD and NAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/NADH_peroxidase NADH peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.1 1.11.1.1] Full crystallographic information is available from [http:// | 2NPX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with <scene name='pdbligand=CYO:'>CYO</scene>, <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/NADH_peroxidase NADH peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.1 1.11.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NPX OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Claiborne, A.]] | [[Category: Claiborne, A.]] | ||
[[Category: Schulz, G | [[Category: Schulz, G E.]] | ||
[[Category: Stehle, T.]] | [[Category: Stehle, T.]] | ||
[[Category: CYO]] | [[Category: CYO]] | ||
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[[Category: oxidoreductase(h2o2(a))]] | [[Category: oxidoreductase(h2o2(a))]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:09:35 2008'' |
Revision as of 19:09, 21 February 2008
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NADH BINDING SITE AND CATALYSIS OF NADH PEROXIDASE
OverviewOverview
The structure of the complex between cofactor NADH and the enzyme NADH peroxidase from Streptococcus faecalis 10C1 (Enterococcus faecalis) has been determined by crystal soaking, X-ray data collection, model building of NADH and refinement at 0.24-nm resolution based on the known enzyme structure [Stehle, T., Ahmed, S. A., Claiborne, A. & Schulz, G. E. (1991) J. Mol. Biol. 221, 1325-1344]. Apart from NADH, the catalytic center of the enzyme contains FAD and a cysteine that shuttles between thiolate and sulfenic acid states. Unfortunately, this cysteine was irreversibly oxidized to a cysteine sulfonic acid in the established enzyme structure. Based on the geometry of the catalytic center, we discuss the stabilization of the oxidation-sensitive sulfenic acid and propose a reaction mechanism.
About this StructureAbout this Structure
2NPX is a Single protein structure of sequence from Enterococcus faecalis with , and as ligands. Active as NADH peroxidase, with EC number 1.11.1.1 Full crystallographic information is available from OCA.
ReferenceReference
NADH binding site and catalysis of NADH peroxidase., Stehle T, Claiborne A, Schulz GE, Eur J Biochem. 1993 Jan 15;211(1-2):221-6. PMID:8425532
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