1qmy
From Proteopedia
(New page: 200px<br /><applet load="1qmy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qmy, resolution 1.90Å" /> '''FMDV LEADER PROTEASE...) |
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| - | [[Image:1qmy.jpg|left|200px]]<br /><applet load="1qmy" size=" | + | [[Image:1qmy.jpg|left|200px]]<br /><applet load="1qmy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qmy, resolution 1.90Å" /> | caption="1qmy, resolution 1.90Å" /> | ||
'''FMDV LEADER PROTEASE (LBSHORT-C51A-C133S)'''<br /> | '''FMDV LEADER PROTEASE (LBSHORT-C51A-C133S)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structures of the two leader protease (Lpro) variants of | + | 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== | ==About this Structure== | ||
| - | 1QMY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus Foot-and-mouth disease virus] with EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1QMY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Foot-and-mouth_disease_virus Foot-and-mouth disease virus] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: sulfhydryl proteinase]] | [[Category: sulfhydryl proteinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:32 2008'' |
Revision as of 12:41, 21 February 2008
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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 with as ligand. 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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