Sandbox Reserved 1059

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[[Image:Image_2_(2).png|100px|left|thumb|Aromatic Amino Acids binding site]]
[[Image:Image_2_(2).png|100px|left|thumb|Aromatic Amino Acids binding site]]
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
 
== Function ==
== Function ==
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== Structure ==
== Structure ==
The tertiary structure of NrdH has a thioredoxin fold with 79 residues with a glutaredoxin-like sequence. However, unlike glutaredoxins, NrdH of ''Mycobacterium tuberculosis'' can accept electrons from thioredoxin reductase. The binding site of NrdH is specific for aromatic amino acids. <ref>DOI 10.1021/bi400191z</ref>
The tertiary structure of NrdH has a thioredoxin fold with 79 residues with a glutaredoxin-like sequence. However, unlike glutaredoxins, NrdH of ''Mycobacterium tuberculosis'' can accept electrons from thioredoxin reductase. The binding site of NrdH is specific for aromatic amino acids. <ref>DOI 10.1021/bi400191z</ref>
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===Conserved Motifs===
===Conserved Motifs===
Members of the NrdH family are typically characterized by CVQC and WSGFRP sequence motifs. The residues between the two cysteines are known to affect redox potentials and pKa values. Also, by changing the target proteins, in turn, they regulate the function. The N-terminal cysteine acts as a nucleophile, whereas the C-terminal cysteine acts as a resolving cysteine. <ref>DOI 10.1021/bi400191z</ref>
Members of the NrdH family are typically characterized by CVQC and WSGFRP sequence motifs. The residues between the two cysteines are known to affect redox potentials and pKa values. Also, by changing the target proteins, in turn, they regulate the function. The N-terminal cysteine acts as a nucleophile, whereas the C-terminal cysteine acts as a resolving cysteine. <ref>DOI 10.1021/bi400191z</ref>
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Within the CVQC motif, the amide oxygen of glutamine residue is firmly hydrogen bonded with the peptidyl nitrogen of Phe-44. The amide nitrogen of glutamine is then available for further hydrogen bonding. The carbonyl oxygen of Val-12 hydrogen bonds with peptidyl nitrogen of Ala-16.
Within the CVQC motif, the amide oxygen of glutamine residue is firmly hydrogen bonded with the peptidyl nitrogen of Phe-44. The amide nitrogen of glutamine is then available for further hydrogen bonding. The carbonyl oxygen of Val-12 hydrogen bonds with peptidyl nitrogen of Ala-16.
<ref>DOI 10.1021/bi400191z</ref>
<ref>DOI 10.1021/bi400191z</ref>
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The WSGFRP motif is stabilized by glutamine of the CVQC motif and phenylalanine is exposed to the solvent. Phe-64 and Val-12 with Ala-16 and Ala-20 create a distinct hydrophobic patch that is exposed to the solvent. This patch is of functional significance that could potentially interact with the C-terminus of RNR. This hydrogen bonding network lends to the stability of the redox active site.<ref>DOI 10.1021/bi400191z</ref>
The WSGFRP motif is stabilized by glutamine of the CVQC motif and phenylalanine is exposed to the solvent. Phe-64 and Val-12 with Ala-16 and Ala-20 create a distinct hydrophobic patch that is exposed to the solvent. This patch is of functional significance that could potentially interact with the C-terminus of RNR. This hydrogen bonding network lends to the stability of the redox active site.<ref>DOI 10.1021/bi400191z</ref>
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[[Image:Image_7_(1).png|100px|left|thumb|Sequence alignment of NrdH from ''Mycobacterium tuberculosis'', ''Corynebacterium glutamicum'', and ''Echerichia coli'']]
[[Image:Image_7_(1).png|100px|left|thumb|Sequence alignment of NrdH from ''Mycobacterium tuberculosis'', ''Corynebacterium glutamicum'', and ''Echerichia coli'']]
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 12:32, 7 April 2015

This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080.
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NrdH of Mycobacterium tuberculosis

NrdH is a redox protein part of a family of redox proteins. The other proteins that maintain the redox balance of this protein are three Thioredoxin and three glutaredoxin-like proteins. Prokaryotes typically maintain redox homeostasis through low-molecular weight thiols (glutathione) and through proteins invovled in disulfide exchange (thioredoxins).

Caption for this structure

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References

  1. ↑ Phulera S, Mande SC. The Crystal Structure of Mycobacterium tuberculosis NrdH at 0.87 A Suggests a Possible Mode of Its Activity. Biochemistry. 2013 May 28. PMID:23675692 doi:10.1021/bi400191z
  2. ↑ Phulera S, Mande SC. The Crystal Structure of Mycobacterium tuberculosis NrdH at 0.87 A Suggests a Possible Mode of Its Activity. Biochemistry. 2013 May 28. PMID:23675692 doi:10.1021/bi400191z
  3. ↑ Phulera S, Mande SC. The Crystal Structure of Mycobacterium tuberculosis NrdH at 0.87 A Suggests a Possible Mode of Its Activity. Biochemistry. 2013 May 28. PMID:23675692 doi:10.1021/bi400191z
  4. ↑ Phulera S, Mande SC. The Crystal Structure of Mycobacterium tuberculosis NrdH at 0.87 A Suggests a Possible Mode of Its Activity. Biochemistry. 2013 May 28. PMID:23675692 doi:10.1021/bi400191z
  5. ↑ Phulera S, Mande SC. The Crystal Structure of Mycobacterium tuberculosis NrdH at 0.87 A Suggests a Possible Mode of Its Activity. Biochemistry. 2013 May 28. PMID:23675692 doi:10.1021/bi400191z
  6. ↑ Phulera S, Mande SC. The Crystal Structure of Mycobacterium tuberculosis NrdH at 0.87 A Suggests a Possible Mode of Its Activity. Biochemistry. 2013 May 28. PMID:23675692 doi:10.1021/bi400191z
  7. ↑ Phulera S, Mande SC. The Crystal Structure of Mycobacterium tuberculosis NrdH at 0.87 A Suggests a Possible Mode of Its Activity. Biochemistry. 2013 May 28. PMID:23675692 doi:10.1021/bi400191z
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