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1l30

From Proteopedia

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REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY

Structural highlights

1l30 is a 1 chain structure with sequence from Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.7Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ENLYS_BPT4 Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.^[1]

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

To investigate the relation between protein stability and the predicted stabilities of individual secondary structural elements, residue Pro86 in an alpha-helix in phage T4 lysozyme was replaced by ten different amino acids. The x-ray crystal structures of seven of the mutant lysozymes were determined at high resolution. In each case, replacement of the proline resulted in the formation of an extended alpha-helix. This involves a large conformational change in residues 81 to 83 and smaller shifts that extend 20 angstroms across the protein surface. Unexpectedly, all ten amino acid substitutions marginally reduce protein thermostability. This insensitivity of stability to the amino acid at position 86 is not simply explained by statistical and thermodynamic criteria for helical propensity. The observed conformational changes illustrate a general mechanism by which proteins can tolerate mutations.

Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.,Alber T, Bell JA, Sun DP, Nicholson H, Wozniak JA, Cook S, Matthews BW Science. 1988 Feb 5;239(4840):631-5. PMID:3277275^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Moussa SH, Kuznetsov V, Tran TA, Sacchettini JC, Young R. Protein determinants of phage T4 lysis inhibition. Protein Sci. 2012 Apr;21(4):571-82. doi: 10.1002/pro.2042. Epub 2012 Mar 2. PMID:22389108 doi:http://dx.doi.org/10.1002/pro.2042
↑ Alber T, Bell JA, Sun DP, Nicholson H, Wozniak JA, Cook S, Matthews BW. Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. Science. 1988 Feb 5;239(4840):631-5. PMID:3277275

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1l30"

Categories: Escherichia virus T4 | Large Structures | Bell JA | Dao-Pin S | Matthews BW

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1l30]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L30 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l30 OCA], [https://pdbe.org/1l30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l30 RCSB], [https://www.ebi.ac.uk/pdbsum/1l30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l30 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l30 OCA], [https://pdbe.org/1l30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l30 RCSB], [https://www.ebi.ac.uk/pdbsum/1l30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l30 ProSAT]</span></td></tr>
 </table>
 == Function ==

1l30

From Proteopedia

Current revision

REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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