1cx6
From Proteopedia
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|PDB= 1cx6 |SIZE=350|CAPTION= <scene name='initialview01'>1cx6</scene>, resolution 2.01Å | |PDB= 1cx6 |SIZE=350|CAPTION= <scene name='initialview01'>1cx6</scene>, resolution 2.01Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span> |
| - | |GENE= GENE E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | |GENE= GENE E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4]) |
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cx6 OCA], [http://www.ebi.ac.uk/pdbsum/1cx6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cx6 RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CX6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1CX6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CX6 OCA]. |
==Reference== | ==Reference== | ||
Substitution with selenomethionine can enhance the stability of methionine-rich proteins., Gassner NC, Baase WA, Hausrath AC, Matthews BW, J Mol Biol. 1999 Nov 19;294(1):17-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10556025 10556025] | Substitution with selenomethionine can enhance the stability of methionine-rich proteins., Gassner NC, Baase WA, Hausrath AC, Matthews BW, J Mol Biol. 1999 Nov 19;294(1):17-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10556025 10556025] | ||
| - | [[Category: | + | [[Category: Enterobacteria phage t4]] |
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Gassner, N C.]] | [[Category: Gassner, N C.]] | ||
[[Category: Matthews, B W.]] | [[Category: Matthews, B W.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: HED]] | ||
[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
[[Category: protein engineering]] | [[Category: protein engineering]] | ||
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[[Category: t4 lysozyme]] | [[Category: t4 lysozyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:30:19 2008'' |
Revision as of 16:30, 30 March 2008
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| , resolution 2.01Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | GENE E (Enterobacteria phage T4) | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
T4 LYSOZYME SUBSTITUTED WITH SELENOMETHIONINE
Overview
The availability of a series of phage T4 lysozymes with up to 14 methionine residues incorporated within the protein has made it possible to systematically compare the effect on protein stability of selenomethionine relative to methionine. Wild-type lysozyme contains two fully buried methionine residues plus three more on the surface. The substitution of these methionine residues with selenomethionine slightly stabilizes the protein. As more and more methionine residues are substituted into the protein, there is a progressive loss of stability. This is, however, increasingly offset in the selenomethionine variants, ultimately resulting in a differential increase in melting temperature of about 7 degrees C. This increase, corresponding to about 0.25 kcal/mol per substitution, is in reasonable agreement with the difference in the solvent transfer free energy between the two amino acids.
About this Structure
1CX6 is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
Reference
Substitution with selenomethionine can enhance the stability of methionine-rich proteins., Gassner NC, Baase WA, Hausrath AC, Matthews BW, J Mol Biol. 1999 Nov 19;294(1):17-20. PMID:10556025
Page seeded by OCA on Sun Mar 30 19:30:19 2008
