1l19

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[[Image:1l19.jpg|left|200px]]<br /><applet load="1l19" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l19.jpg|left|200px]]
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caption="1l19, resolution 1.7&Aring;" />
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'''ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES'''<br />
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{{Structure
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|PDB= 1l19 |SIZE=350|CAPTION= <scene name='initialview01'>1l19</scene>, resolution 1.7&Aring;
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|SITE=
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|LIGAND=
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|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]
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|GENE=
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}}
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'''ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1L19 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=1L19 OCA].
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1L19 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L19 OCA].
==Reference==
==Reference==
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Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles., Nicholson H, Becktel WJ, Matthews BW, Nature. 1988 Dec 15;336(6200):651-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3200317 3200317]
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Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles., Nicholson H, Becktel WJ, Matthews BW, Nature. 1988 Dec 15;336(6200):651-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/3200317 3200317]
[[Category: Bacteriophage t4]]
[[Category: Bacteriophage t4]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: hydrolase (o-glycosyl)]]
[[Category: hydrolase (o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:24:58 2008''

Revision as of 10:24, 20 March 2008

Image:1l19.jpg


PDB ID 1l19

Drag the structure with the mouse to rotate
, resolution 1.7Å
Activity: Lysozyme, with EC number 3.2.1.17
Coordinates: save as pdb, mmCIF, xml



ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES


Overview

Two different genetically engineered amino-acid substitutions designed to interact with alpha-helix dipoles in T4 lysozyme are shown to increase the thermal stability of the protein. Crystallographic analyses of the mutant lysozyme structures suggest that the stabilization is due to electrostatic interaction and does not require precise hydrogen bonding between the substituted amino acid and the end of the alpha-helix.

About this Structure

1L19 is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.

Reference

Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles., Nicholson H, Becktel WJ, Matthews BW, Nature. 1988 Dec 15;336(6200):651-6. PMID:3200317

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