1kni
From Proteopedia
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|PDB= 1kni |SIZE=350|CAPTION= <scene name='initialview01'>1kni</scene>, resolution 1.7Å | |PDB= 1kni |SIZE=350|CAPTION= <scene name='initialview01'>1kni</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kni OCA], [http://www.ebi.ac.uk/pdbsum/1kni PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kni RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KNI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1KNI 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=1KNI OCA]. |
==Reference== | ==Reference== | ||
Structure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme., Jacobson RH, Matsumura M, Faber HR, Matthews BW, Protein Sci. 1992 Jan;1(1):46-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1304882 1304882] | Structure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme., Jacobson RH, Matsumura M, Faber HR, Matthews BW, Protein Sci. 1992 Jan;1(1):46-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1304882 1304882] | ||
| - | [[Category: | + | [[Category: Enterobacteria phage t4]] |
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Matsumura, M.]] | [[Category: Matsumura, M.]] | ||
[[Category: Matthews, B W.]] | [[Category: Matthews, B W.]] | ||
| - | [[Category: BME]] | ||
| - | [[Category: CL]] | ||
[[Category: bacteriolytic enzyme]] | [[Category: bacteriolytic enzyme]] | ||
[[Category: glycosidase]] | [[Category: glycosidase]] | ||
| - | ''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 21:51:01 2008'' |
Revision as of 18:51, 30 March 2008
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| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Stabilizing Disulfide Bridge Mutant of T4 Lysozyme
Overview
The engineered disulfide bridge between residues 21 and 142 of phage T4 lysozyme spans the active-site cleft and can be used as a switch to control the activity of the enzyme (Matsumura, M. & Matthews, B.W., 1989, Science 243, 792-794). In the oxidized form the disulfide increases the melting temperature of the protein by 11 degrees C at pH 2. The crystal structure of this mutant lysozyme has been determined in both the reduced and oxidized forms. In the reduced form, the crystal structure of the mutant is shown to be extremely similar to that of wild type. In the oxidized form, however, the formation of the disulfide bridge causes the alpha-carbons of Cys 21 and Cys 142, on opposite sides of the active-site cleft, to move toward each other by 2.5 A. In association with this movement, the amino-terminal domain of the protein undergoes a rigid-body rotation of 5.1 degrees relative to the carboxy-terminal domain. This rotation occurs about an axis passing through the junction of the amino-terminal and carboxy-terminal domains and is also close to the axis that best fits the apparent thermal motion of the amino-terminal domain seen previously in crystals of wild-type lysozyme. Even though the engineered Cys 21-Cys 142 disulfide links together the amino-terminal and carboxy-terminal domains of T4 lysozyme, it does not reduce the apparent mobility of the one domain relative to the other. The pronounced "hinge-bending" mobility of the amino-terminal domain that is suggested by the crystallographic thermal parameters of wild-type lysozyme persists in the oxidized (and reduced) mutant structures. In the immediate vicinity of the introduced disulfide bridge the mutant structure is more mobile (or disordered) than wild type, so much so that the exact conformation of Cys 21 remains obscure. As with the previously described disulfide bridge between residues 9 and 164 of T4 lysozyme (Pjura, P.E., Matsumura, M., Wozniak, J.A., & Matthews, B.W., 1990, Biochemistry 29, 2592-2598), the engineered cross-link substantially enhances the stability of the protein without making the folded structure more rigid.
About this Structure
1KNI is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
Reference
Structure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme., Jacobson RH, Matsumura M, Faber HR, Matthews BW, Protein Sci. 1992 Jan;1(1):46-57. PMID:1304882
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