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[[Image:1l12.png|left|200px]]
==CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME==
<StructureSection load='1l12' size='340' side='right' caption='[[1l12]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1l12]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L12 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lzm|2lzm]], [[1l01|1l01]], [[1l02|1l02]], [[1l03|1l03]], [[1l04|1l04]], [[1l05|1l05]], [[1l06|1l06]], [[1l07|1l07]], [[1l08|1l08]], [[1l09|1l09]], [[1l10|1l10]], [[1l11|1l11]], [[1l13|1l13]], [[1l14|1l14]], [[1l15|1l15]], [[1l16|1l16]], [[1l17|1l17]], [[1l18|1l18]], [[1l19|1l19]], [[1l20|1l20]], [[1l21|1l21]], [[1l22|1l22]], [[1l23|1l23]], [[1l24|1l24]], [[1l25|1l25]], [[1l26|1l26]], [[1l27|1l27]], [[1l28|1l28]], [[1l29|1l29]], [[1l30|1l30]], [[1l31|1l31]], [[1l32|1l32]], [[1l33|1l33]], [[1l34|1l34]], [[1l35|1l35]], [[1l36|1l36]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l12 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1l12 RCSB], [http://www.ebi.ac.uk/pdbsum/1l12 PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l1/1l12_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


{{STRUCTURE_1l12|  PDB=1l12  |  SCENE=  }}
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<ref>PMID:3118211</ref>


===CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_3118211}}
 
==About this Structure==
[[1l12]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L12 OCA].


==See Also==
==See Also==
*[[Hen Egg-White (HEW) Lysozyme|Hen Egg-White (HEW) Lysozyme]]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:003118211</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Enterobacteria phage t4]]
[[Category: Enterobacteria phage t4]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]

Revision as of 18:37, 28 September 2014

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

1l12 is a 1 chain structure with sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:2lzm, 1l01, 1l02, 1l03, 1l04, 1l05, 1l06, 1l07, 1l08, 1l09, 1l10, 1l11, 1l13, 1l14, 1l15, 1l16, 1l17, 1l18, 1l19, 1l20, 1l21, 1l22, 1l23, 1l24, 1l25, 1l26, 1l27, 1l28, 1l29, 1l30, 1l31, 1l32, 1l33, 1l34, 1l35, 1l36
Activity:Lysozyme, with EC number 3.2.1.17
Resources:FirstGlance, OCA, RCSB, PDBsum

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 PubMed

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.

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 Also

References

  1. ↑ Alber T, Sun DP, Wilson K, Wozniak JA, Cook SP, Matthews BW. Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature. 1987 Nov 5-11;330(6143):41-6. PMID:3118211 doi:http://dx.doi.org/10.1038/330041a0

1l12, resolution 1.70Å

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