1lvb
From Proteopedia
(New page: 200px<br /><applet load="1lvb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lvb, resolution 2.20Å" /> '''CATALYTICALLY INACTI...) |
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| - | [[Image:1lvb.gif|left|200px]]<br /><applet load="1lvb" size=" | + | [[Image:1lvb.gif|left|200px]]<br /><applet load="1lvb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lvb, resolution 2.20Å" /> | caption="1lvb, resolution 2.20Å" /> | ||
'''CATALYTICALLY INACTIVE TOBACCO ETCH VIRUS PROTEASE COMPLEXED WITH SUBSTRATE'''<br /> | '''CATALYTICALLY INACTIVE TOBACCO ETCH VIRUS PROTEASE COMPLEXED WITH SUBSTRATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Because of its stringent sequence specificity, the 3C-type protease from | + | Because of its stringent sequence specificity, the 3C-type protease from tobacco etch virus (TEV) is frequently used to remove affinity tags from recombinant proteins. It is unclear, however, exactly how TEV protease recognizes its substrates with such high selectivity. The crystal structures of two TEV protease mutants, inactive C151A and autolysis-resistant S219D, have now been solved at 2.2- and 1.8-A resolution as complexes with a substrate and product peptide, respectively. The enzyme does not appear to have been perturbed by the mutations in either structure, and the modes of binding of the product and substrate are virtually identical. Analysis of the protein-ligand interactions helps to delineate the structural determinants of substrate specificity and provides guidance for reengineering the enzyme to further improve its utility for biotechnological applications. |
==About this Structure== | ==About this Structure== | ||
| - | 1LVB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Tobacco_etch_virus Tobacco etch virus] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1LVB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Tobacco_etch_virus Tobacco etch virus] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LVB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Tobacco etch virus]] | [[Category: Tobacco etch virus]] | ||
| - | [[Category: Evdokimov, A | + | [[Category: Evdokimov, A G.]] |
| - | [[Category: III, H | + | [[Category: III, H K.Peters.]] |
| - | [[Category: Kapust, R | + | [[Category: Kapust, R B.]] |
[[Category: Li, M.]] | [[Category: Li, M.]] | ||
[[Category: Phan, J.]] | [[Category: Phan, J.]] | ||
| - | [[Category: Tropea, J | + | [[Category: Tropea, J E.]] |
| - | [[Category: Waugh, D | + | [[Category: Waugh, D S.]] |
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
[[Category: Zdanov, A.]] | [[Category: Zdanov, A.]] | ||
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[[Category: protein-peptide complex]] | [[Category: protein-peptide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:47 2008'' |
Revision as of 11:48, 21 February 2008
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CATALYTICALLY INACTIVE TOBACCO ETCH VIRUS PROTEASE COMPLEXED WITH SUBSTRATE
Overview
Because of its stringent sequence specificity, the 3C-type protease from tobacco etch virus (TEV) is frequently used to remove affinity tags from recombinant proteins. It is unclear, however, exactly how TEV protease recognizes its substrates with such high selectivity. The crystal structures of two TEV protease mutants, inactive C151A and autolysis-resistant S219D, have now been solved at 2.2- and 1.8-A resolution as complexes with a substrate and product peptide, respectively. The enzyme does not appear to have been perturbed by the mutations in either structure, and the modes of binding of the product and substrate are virtually identical. Analysis of the protein-ligand interactions helps to delineate the structural determinants of substrate specificity and provides guidance for reengineering the enzyme to further improve its utility for biotechnological applications.
About this Structure
1LVB is a Protein complex structure of sequences from Tobacco etch virus with as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for the substrate specificity of tobacco etch virus protease., Phan J, Zdanov A, Evdokimov AG, Tropea JE, Peters HK 3rd, Kapust RB, Li M, Wlodawer A, Waugh DS, J Biol Chem. 2002 Dec 27;277(52):50564-72. Epub 2002 Oct 10. PMID:12377789
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