User:Ashley Steere/Sandbox 1
From Proteopedia
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===Structure of TEV Protease=== | ===Structure of TEV Protease=== | ||
| - | TEV protease adopts a two-domain antiparallel [http://en.wikipedia.org/wiki/Beta_barrel β-barrel] fold, typical of trypsin-like serine proteases. Located at the interface between the two domains is the catalytic triad, composed of His46, Asp81, and Cys151. A structural comparison with related proteins reveals that the TEV protease fold is most similar to that of the 3C [http://en.wikipedia.org/wiki/Cysteine_protease cysteine proteases] from [http://proteopedia.org/wiki/index.php/1hav hepatitis A virus] and rhinovirus, which serve a similar function as the TEV protease in their respective viruses. However, although the overall fold of TEV protease and these related proteins is indeed very similar, the actual atomic coordinates are very different, with the root mean square deviation for Cα carbons between 2.4 to 3.5Å. | + | TEV protease adopts a two-domain antiparallel [http://en.wikipedia.org/wiki/Beta_barrel β-barrel] fold, typical of trypsin-like serine proteases. Located at the interface between the two domains is the catalytic triad, composed of His46, Asp81, and Cys151. A structural comparison with related proteins reveals that the TEV protease fold is most similar to that of the 3C [http://en.wikipedia.org/wiki/Cysteine_protease cysteine proteases] from [http://proteopedia.org/wiki/index.php/1hav hepatitis A virus] and [http://proteopedia.org/wiki/index.php/1cqq rhinovirus], which serve a similar function as the TEV protease in their respective viruses. However, although the overall fold of TEV protease and these related proteins is indeed very similar, the actual atomic coordinates are very different, with the root mean square deviation for Cα carbons between 2.4 to 3.5Å. |
Revision as of 20:10, 27 March 2009
Tobacco Etch Virus (TEV) Protease
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The tobacco etch virus (TEV) is a member of the Potyviridae family of RNA viruses. The RNA genome of the TEV is translated into a large polyprotein precursor that is cleaved soon after translation to form independent protein products. The TEV nuclear inclusion a (NIa) protease is a 27 kDa 3C-type protease responsible for the processing of the original polyprotein into functional viral proteins. TEV protease resembles well-known serine proteases, such as trypsin and chymotrypsin, except that the TEV protease utilizes the nucleophilic thiol of the active site cysteine residue, as opposed to the serine hydroxyl used in serine proteases. Ultimately, the biological importance of the TEV protease requires that the enzyme have very stringent sequence specificity to ensure proper production of viral proteins, and it is for this reason that the TEV protease has increasingly been used to remove affinity tags from recombinant proteins.
Structure of TEV Protease
TEV protease adopts a two-domain antiparallel β-barrel fold, typical of trypsin-like serine proteases. Located at the interface between the two domains is the catalytic triad, composed of His46, Asp81, and Cys151. A structural comparison with related proteins reveals that the TEV protease fold is most similar to that of the 3C cysteine proteases from hepatitis A virus and rhinovirus, which serve a similar function as the TEV protease in their respective viruses. However, although the overall fold of TEV protease and these related proteins is indeed very similar, the actual atomic coordinates are very different, with the root mean square deviation for Cα carbons between 2.4 to 3.5Å.
