1qmy
From Proteopedia
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| - | [[Image:1qmy.jpg|left|200px]] | + | [[Image:1qmy.jpg|left|200px]] |
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| - | '''FMDV LEADER PROTEASE (LBSHORT-C51A-C133S)''' | + | {{Structure |
| + | |PDB= 1qmy |SIZE=350|CAPTION= <scene name='initialview01'>1qmy</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''FMDV LEADER PROTEASE (LBSHORT-C51A-C133S)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QMY is a [ | + | 1QMY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus Foot-and-mouth disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMY OCA]. |
==Reference== | ==Reference== | ||
| - | Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes., Guarne A, Hampoelz B, Glaser W, Carpena X, Tormo J, Fita I, Skern T, J Mol Biol. 2000 Oct 6;302(5):1227-40. PMID:[http:// | + | Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes., Guarne A, Hampoelz B, Glaser W, Carpena X, Tormo J, Fita I, Skern T, J Mol Biol. 2000 Oct 6;302(5):1227-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11183785 11183785] |
[[Category: Foot-and-mouth disease virus]] | [[Category: Foot-and-mouth disease virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sulfhydryl proteinase]] | [[Category: sulfhydryl proteinase]] | ||
| - | ''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 13:39:52 2008'' |
Revision as of 11:39, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
FMDV LEADER PROTEASE (LBSHORT-C51A-C133S)
Overview
The structures of the two leader protease (Lpro) variants of foot-and-mouth disease virus known to date were solved using crystals in which molecules were organized as molecular fibers. Such crystals diffract to a resolution of only approximately 3 A. This singular, pseudo-polymeric organization is present in a new Lpro crystal form showing a cubic packing. As molecular fiber formation appeared unrelated to crystallization conditions, we mutated the reactive cysteine 133 residue, which makes a disulfide bridge between adjacent monomers in the fibers, to serine. None of the intermolecular contacts found in the molecular fibers was present in crystals of this variant. Analysis of this Lpro structure, refined at 1.9 A resolution, enables a detailed definition of the active center of the enzyme, including the solvent organization. Assay of Lpro activity on a fluorescent hexapeptide substrate showed that Lpro, in contrast to papain, was highly sensitive to increases in the cation concentration and was active only across a narrow pH range. Examination of the Lpro structure revealed that three aspartate residues near the active site, not present in papain-like enzymes, are probably responsible for these properties.
About this Structure
1QMY is a Single protein structure of sequence from Foot-and-mouth disease virus. Full crystallographic information is available from OCA.
Reference
Structural and biochemical features distinguish the foot-and-mouth disease virus leader proteinase from other papain-like enzymes., Guarne A, Hampoelz B, Glaser W, Carpena X, Tormo J, Fita I, Skern T, J Mol Biol. 2000 Oct 6;302(5):1227-40. PMID:11183785
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