1l03
From Proteopedia
(New page: 200px<br /><applet load="1l03" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l03, resolution 1.7Å" /> '''CONTRIBUTIONS OF HYDR...) |
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| - | [[Image:1l03.jpg|left|200px]]<br /><applet load="1l03" size=" | + | [[Image:1l03.jpg|left|200px]]<br /><applet load="1l03" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l03, resolution 1.7Å" /> | caption="1l03, resolution 1.7Å" /> | ||
'''CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME'''<br /> | '''CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Measurements of changes in structure and stability caused by 13 different | + | Measurements of changes in structure and stability caused by 13 different substitutions for threonine 157 in phage T4 lysozyme show that the most stable lysozyme variants contain hydrogen bonds analogous to those in the wild-type enzyme and that structural adjustments allow the protein to be surprisingly tolerant of amino-acid substitutions. |
==About this Structure== | ==About this Structure== | ||
| - | 1L03 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with BME as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1L03 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1L03 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Alber, T.]] | [[Category: Alber, T.]] | ||
[[Category: Dao-Pin, S.]] | [[Category: Dao-Pin, S.]] | ||
| - | [[Category: Matthews, B | + | [[Category: Matthews, B W.]] |
[[Category: Wilson, K.]] | [[Category: Wilson, K.]] | ||
[[Category: BME]] | [[Category: BME]] | ||
[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:49 2008'' |
Revision as of 11:39, 21 February 2008
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CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Overview
Measurements of changes in structure and stability caused by 13 different substitutions for threonine 157 in phage T4 lysozyme show that the most stable lysozyme variants contain hydrogen bonds analogous to those in the wild-type enzyme and that structural adjustments allow the protein to be surprisingly tolerant of amino-acid substitutions.
About this Structure
1L03 is a Single protein structure of sequence from Bacteriophage t4 with as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme., Alber T, Sun DP, Wilson K, Wozniak JA, Cook SP, Matthews BW, Nature. 1987 Nov 5-11;330(6143):41-6. PMID:3118211
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