1l03

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[[Image:1l03.jpg|left|200px]]<br /><applet load="1l03" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l03.jpg|left|200px]]
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caption="1l03, resolution 1.7&Aring;" />
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'''CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME'''<br />
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{{Structure
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|PDB= 1l03 |SIZE=350|CAPTION= <scene name='initialview01'>1l03</scene>, resolution 1.7&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
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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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'''CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1L03 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=1L03 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3118211 3118211]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/3118211 3118211]
[[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 13:39:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:24:37 2008''

Revision as of 10:24, 20 March 2008

Image:1l03.jpg


PDB ID 1l03

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



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. 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

Page seeded by OCA on Thu Mar 20 12:24:37 2008

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