1l05: Difference between revisions
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==CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME== | ==CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME== | ||
<StructureSection load='1l05' size='340' side='right' caption='[[1l05]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='1l05' size='340' side='right'caption='[[1l05]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1l05]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L05 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1l05]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L05 FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l0/1l05_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l0/1l05_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bpt4]] | [[Category: Bpt4]] | ||
[[Category: Large Structures]] | |||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Alber, T]] | [[Category: Alber, T]] | ||
[[Category: Dao-Pin, S]] | [[Category: Dao-Pin, S]] | ||
[[Category: Matthews, B W]] | [[Category: Matthews, B W]] | ||
Revision as of 15:25, 13 November 2019
CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYMECONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME
Structural highlights
Function[LYS_BPT4] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMeasurements 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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