1l03

From Proteopedia

(Difference between revisions)

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 ==CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME==
 <StructureSection load='1l03' size='340' side='right' caption='[[1l03]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lzm|2lzm]], [[1l01|1l01]], [[1l02|1l02]], [[1l04|1l04]], [[1l05|1l05]], [[1l06|1l06]], [[1l07|1l07]], [[1l08|1l08]], [[1l09|1l09]], [[1l10|1l10]], [[1l11|1l11]], [[1l12|1l12]], [[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 id='activity'><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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l03 OCA], [http://pdbe.org/1l03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l03 RCSB], [http://www.ebi.ac.uk/pdbsum/1l03 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l03 OCA], [http://pdbe.org/1l03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l03 RCSB], [http://www.ebi.ac.uk/pdbsum/1l03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l03 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <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].
+</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/main_output.php?pdb_ID=1l03 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

Revision as of 10:51, 18 October 2017

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME

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1l03, resolution 1.70Å

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Structural highlights

1l03 is a 1 chain structure with sequence from Bpt4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2lzm, 1l01, 1l02, 1l04, 1l05, 1l06, 1l07, 1l08, 1l09, 1l10, 1l11, 1l12, 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, PDBe, RCSB, PDBsum, ProSAT

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 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.

References

↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

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1l03

From Proteopedia

Revision as of 10:51, 18 October 2017

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

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