User:Eduarda Franco Marcolino/Sandbox 1

From Proteopedia

(Difference between revisions)

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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 =Reactive oxygen species (ROS) and nitrogen intermediates can cause cellular damage. Cells have developed several mechanisms to eliminate these reactive molecules or repair the damage. Among proteins, one of the amino acids most easily oxidized is methionine, which is converted into methionine sulfoxide. The enzyme peptide methionine sulfoxide reductase (MsrA) catalyzes the reduction of methionine sulfoxide back to methionine, both in proteins and as free methionine. MsrA plays an important role in protecting the cell against oxidative damage.=
+== Function ==
+Reactive oxygen species (ROS) and nitrogen intermediates can cause cellular damage. Cells have developed several mechanisms to eliminate these reactive molecules or repair the damage. Among proteins, one of the amino acids most easily oxidized is methionine, which is converted into methionine sulfoxide. The enzyme peptide methionine sulfoxide reductase (MsrA) catalyzes the reduction of methionine sulfoxide back to methionine, both in proteins and as free methionine. MsrA plays an important role in protecting the cell against oxidative damage.
 == Disease ==
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 == Relevance ==
-== Structural highlights =n. There are three cysteine residues located in the vicinity of the active site. Conformational changes in a glycine-rich C-terminal tail appear to allow all three thiols to come together and to participate in catalysis. The structures support a unique, thiol-disulfide exchange mechanism that relies upon an essential cysteine as a nucleophile and additional conserved residues that interact with the oxygen atom of the sulfoxide moiety. MsrAs contain within their presumed active sites a conserved Gly-Cys-Phe-Trp-Gly motif =
+== Structural highlights ==
+There are three cysteine residues located in the vicinity of the active site. Conformational changes in a glycine-rich C-terminal tail appear to allow all three thiols to come together and to participate in catalysis. The structures support a unique, thiol-disulfide exchange mechanism that relies upon an essential cysteine as a nucleophile and additional conserved residues that interact with the oxygen atom of the sulfoxide moiety. MsrAs contain within their presumed active sites a conserved Gly-Cys-Phe-Trp-Gly motif
 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>
-== References =Lowther, W. T, et al. “Structure and Mechanism of Peptide Methionine Sulfoxide Reductase, an “Anti-Oxidation” Enzyme,.” Biochemistry, vol. 39, no. 44, 13 Oct. 2000, pp. 13307–13312, https://doi.org/10.1021/bi0020269. Accessed 1 Aug. 2022.=
+== References ==
+Lowther, W. T, et al. “Structure and Mechanism of Peptide Methionine Sulfoxide Reductase, an “Anti-Oxidation” Enzyme,.” Biochemistry, vol. 39, no. 44, 13 Oct. 2000, pp. 13307–13312, https://doi.org/10.1021/bi0020269. Accessed 1 Aug. 2022.
 <references/>

Revision as of 10:55, 7 June 2025

==Your Heading Here (maybe something like 'Structure')= BOVINE METHIONINE SULFOXIDE REDUCTASE =

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You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

1 Function
2 Disease
3 Relevance
4 Structural highlights

Function

Reactive oxygen species (ROS) and nitrogen intermediates can cause cellular damage. Cells have developed several mechanisms to eliminate these reactive molecules or repair the damage. Among proteins, one of the amino acids most easily oxidized is methionine, which is converted into methionine sulfoxide. The enzyme peptide methionine sulfoxide reductase (MsrA) catalyzes the reduction of methionine sulfoxide back to methionine, both in proteins and as free methionine. MsrA plays an important role in protecting the cell against oxidative damage.

Disease

Relevance

Structural highlights

There are three cysteine residues located in the vicinity of the active site. Conformational changes in a glycine-rich C-terminal tail appear to allow all three thiols to come together and to participate in catalysis. The structures support a unique, thiol-disulfide exchange mechanism that relies upon an essential cysteine as a nucleophile and additional conserved residues that interact with the oxygen atom of the sulfoxide moiety. MsrAs contain within their presumed active sites a conserved Gly-Cys-Phe-Trp-Gly motif

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

Lowther, W. T, et al. “Structure and Mechanism of Peptide Methionine Sulfoxide Reductase, an “Anti-Oxidation” Enzyme,.” Biochemistry, vol. 39, no. 44, 13 Oct. 2000, pp. 13307–13312, https://doi.org/10.1021/bi0020269. Accessed 1 Aug. 2022.

↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644