1lvm
From Proteopedia
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| - | [[Image:1lvm.gif|left|200px]] | + | [[Image:1lvm.gif|left|200px]] |
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| - | '''CATALYTICALLY ACTIVE TOBACCO ETCH VIRUS PROTEASE COMPLEXED WITH PRODUCT''' | + | {{Structure |
| + | |PDB= 1lvm |SIZE=350|CAPTION= <scene name='initialview01'>1lvm</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CATALYTICALLY ACTIVE TOBACCO ETCH VIRUS PROTEASE COMPLEXED WITH PRODUCT''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LVM is a [ | + | 1LVM is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Tobacco_etch_virus Tobacco etch virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LVM OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12377789 12377789] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Tobacco etch virus]] | [[Category: Tobacco etch virus]] | ||
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[[Category: enzyme-peptide complex]] | [[Category: enzyme-peptide complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:35:43 2008'' |
Revision as of 10:35, 20 March 2008
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| , resolution 1.80Å | |||||||
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| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CATALYTICALLY ACTIVE TOBACCO ETCH VIRUS PROTEASE COMPLEXED WITH PRODUCT
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
1LVM is a Protein complex structure of sequences from Tobacco etch virus. 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
Page seeded by OCA on Thu Mar 20 12:35:43 2008
