1nhs

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[[Image:1nhs.jpg|left|200px]]<br /><applet load="1nhs" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nhs.jpg|left|200px]]
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caption="1nhs, resolution 2.0&Aring;" />
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'''AN L40C MUTATION CONVERTS THE CYSTEINE-SULFENIC ACID REDOX CENTRE IN ENTEROCOCCAL NADH PEROXIDASE TO A DISULFIDE'''<br />
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{{Structure
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|PDB= 1nhs |SIZE=350|CAPTION= <scene name='initialview01'>1nhs</scene>, resolution 2.0&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=CYO:OXYGENS+BOUND+TO+CYS+SG'>CYO</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''AN L40C MUTATION CONVERTS THE CYSTEINE-SULFENIC ACID REDOX CENTRE IN ENTEROCOCCAL NADH PEROXIDASE TO A DISULFIDE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1NHS 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=SO4:'>SO4</scene>, <scene name='pdbligand=CYO:'>CYO</scene> and <scene name='pdbligand=FAD:'>FAD</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=1NHS OCA].
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1NHS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NHS OCA].
==Reference==
==Reference==
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An L40C mutation converts the cysteine-sulfenic acid redox center in enterococcal NADH peroxidase to a disulfide., Miller H, Mande SS, Parsonage D, Sarfaty SH, Hol WG, Claiborne A, Biochemistry. 1995 Apr 18;34(15):5180-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7711038 7711038]
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An L40C mutation converts the cysteine-sulfenic acid redox center in enterococcal NADH peroxidase to a disulfide., Miller H, Mande SS, Parsonage D, Sarfaty SH, Hol WG, Claiborne A, Biochemistry. 1995 Apr 18;34(15):5180-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7711038 7711038]
[[Category: Enterococcus faecalis]]
[[Category: Enterococcus faecalis]]
[[Category: NADH peroxidase]]
[[Category: NADH peroxidase]]
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[[Category: oxidoreductase (h2o2(a))]]
[[Category: oxidoreductase (h2o2(a))]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:57:05 2008''

Revision as of 10:57, 20 March 2008


PDB ID 1nhs

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands: , and
Activity: NADH peroxidase, with EC number 1.11.1.1
Coordinates: save as pdb, mmCIF, xml



AN L40C MUTATION CONVERTS THE CYSTEINE-SULFENIC ACID REDOX CENTRE IN ENTEROCOCCAL NADH PEROXIDASE TO A DISULFIDE


Overview

Multiple sequence alignments including the enterococcal NADH peroxidase and NADH oxidase indicate that residues Ser38 and Cys42 align with the two cysteines of the redox-active disulfides found in glutathione reductase (GR), lipoamide dehydrogenase, mercuric reductase, and trypanothione reductase. In order to evaluate those structural determinants involved in the selection of the cysteine-sulfenic acid (Cys-SOH) redox centers found in the two peroxide reductases and the redox-active disulfides present in the GR class of disulfide reductases, NADH peroxidase residues Ser38, Phe39, Leu40, and Ser41 have been individually replaced with Cys. Both the F39C and L40C mutant peroxidases yield active-site disulfides involving the new Cys and the native Cys42; formation of the Cys39-Cys42 disulfide, however, precludes binding of the FAD coenzyme. In contrast, the L40C mutant contains tightly-bound FAD and has been analyzed by both kinetic and spectroscopic approaches. In addition, the L40C and S41C mutant structures have been determined at 2.1 and 2.0 A resolution, respectively, by X-ray crystallography. Formation of the Cys40-Cys42 disulfide bond requires a movement of Cys42-SG to a new position 5.9 A from the flavin-C(4a) position; this is consistent with the inability of the new disulfide to function as a redox center in concert with the flavin. Stereochemical constraints prohibit formation of the Cys41-Cys42 disulfide in the latter mutant.

About this Structure

1NHS is a Single protein structure of sequence from Enterococcus faecalis. Full crystallographic information is available from OCA.

Reference

An L40C mutation converts the cysteine-sulfenic acid redox center in enterococcal NADH peroxidase to a disulfide., Miller H, Mande SS, Parsonage D, Sarfaty SH, Hol WG, Claiborne A, Biochemistry. 1995 Apr 18;34(15):5180-90. PMID:7711038

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