256l
From Proteopedia
(New page: 200px<br /><applet load="256l" size="450" color="white" frame="true" align="right" spinBox="true" caption="256l, resolution 1.8Å" /> '''BACTERIOPHAGE T4 LYSO...) |
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| - | [[Image:256l.jpg|left|200px]]<br /><applet load="256l" size=" | + | [[Image:256l.jpg|left|200px]]<br /><applet load="256l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="256l, resolution 1.8Å" /> | caption="256l, resolution 1.8Å" /> | ||
'''BACTERIOPHAGE T4 LYSOZYME'''<br /> | '''BACTERIOPHAGE T4 LYSOZYME'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phage T4 lysozyme consists of two domains between which is formed the | + | Phage T4 lysozyme consists of two domains between which is formed the active-site cleft of the enzyme. The crystallographically determined thermal displacement parameters for the protein suggested that the amino terminal of the two domains undergoes 'hinge-bending' motion about an axis passing through the waist of the molecule. Such conformational mobility may be important in allowing access of substrates to the active site of the enzyme. We report here a crystallographic study of a mutant T4 lysozyme which demonstrates further the conformational flexibility of the protein. A mutant form of the enzyme with a methionine residue (Met 6) replaced by isoleucine crystallizes with four independent molecules in the crystal lattice. These four molecules have distinctly different conformations. The mutant protein can also crystallize in standard form with a structure very similar to the wild-type protein. Thus the mutant protein can adopt five different crystal conformations. The isoleucine for methionine substitution at the intersection of the two domains of T4 lysozyme apparently enhances the hinge-bending motion presumed to occur in the wild-type protein, without significantly affecting the catalytic activity or thermal stability of the protein. |
==About this Structure== | ==About this Structure== | ||
| - | 256L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Active as [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] Full crystallographic information is available from [http:// | + | 256L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=256L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Faber, H | + | [[Category: Faber, H R.]] |
| - | [[Category: Matthews, B | + | [[Category: Matthews, B W.]] |
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: lysozyme]] | [[Category: lysozyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:21:50 2008'' |
Revision as of 14:21, 21 February 2008
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BACTERIOPHAGE T4 LYSOZYME
Overview
Phage T4 lysozyme consists of two domains between which is formed the active-site cleft of the enzyme. The crystallographically determined thermal displacement parameters for the protein suggested that the amino terminal of the two domains undergoes 'hinge-bending' motion about an axis passing through the waist of the molecule. Such conformational mobility may be important in allowing access of substrates to the active site of the enzyme. We report here a crystallographic study of a mutant T4 lysozyme which demonstrates further the conformational flexibility of the protein. A mutant form of the enzyme with a methionine residue (Met 6) replaced by isoleucine crystallizes with four independent molecules in the crystal lattice. These four molecules have distinctly different conformations. The mutant protein can also crystallize in standard form with a structure very similar to the wild-type protein. Thus the mutant protein can adopt five different crystal conformations. The isoleucine for methionine substitution at the intersection of the two domains of T4 lysozyme apparently enhances the hinge-bending motion presumed to occur in the wild-type protein, without significantly affecting the catalytic activity or thermal stability of the protein.
About this Structure
256L is a Single protein structure of sequence from Bacteriophage t4. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
A mutant T4 lysozyme displays five different crystal conformations., Faber HR, Matthews BW, Nature. 1990 Nov 15;348(6298):263-6. PMID:2234094
Page seeded by OCA on Thu Feb 21 16:21:50 2008
