5ki2: Difference between revisions
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==PSEUDO T4 LYSOZYME MUTANT - Y18PHE-METHYL== | |||
<StructureSection load='5ki2' size='340' side='right'caption='[[5ki2]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ki2]] 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=5KI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KI2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4PH:4-METHYL-L-PHENYLALANINE'>4PH</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene></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=5ki2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ki2 OCA], [https://pdbe.org/5ki2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ki2 RCSB], [https://www.ebi.ac.uk/pdbsum/5ki2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ki2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ENLYS_BPT4 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.<ref>PMID:22389108</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structures and stabilities of proteins are defined by a series of weak non-covalent electrostatic, van der Waals, and hydrogen bond (HB) interactions. In this study, we have designed and engineered halogen bonds (XBs) site-specifically in order to study their structure-energy relationship in a model protein, T4 lysozyme. The evidence for XBs is the displacement of the aromatic side chain towards an oxygen acceptor, at distances that are at or less than the sums of their respective van der Waals radii, when the hydroxyl substituent of the wildtype tyrosine is replaced by an iodine. In addition, thermal melting studies show that the iodine XB rescues the stabilization energy from an otherwise destabilizing substitution (at an equivalent non-interacting site), indicating that the interaction is also present in solution. Quantum chemical calculations show that the XB complements an HB at this site and that solvent structure must also be considered in trying to design molecular interactions such as XBs into biological systems. A bromine substitution also shows displacement of the side chain, but the distances and geometries do not indicate formation of an XB. Thus, we have dissected the contributions from various non-covalent interactions of halogens introduced into proteins, to drive the application of XBs, particularly in biomolecular design. | |||
Structure-Energy Relationships of Halogen Bonds in Proteins.,Scholfield MR, Ford MC, Carlsson AC, Butta H, Mehl RA, Ho PS Biochemistry. 2017 Mar 27. doi: 10.1021/acs.biochem.7b00022. PMID:28345933<ref>PMID:28345933</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Ford | <div class="pdbe-citations 5ki2" style="background-color:#fffaf0;"></div> | ||
[[Category: Scholfield | |||
==See Also== | |||
*[[Lysin 3D structures|Lysin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia virus T4]] | |||
[[Category: Large Structures]] | |||
[[Category: Ford MC]] | |||
[[Category: Scholfield MR]] | |||
Latest revision as of 13:01, 27 September 2023
PSEUDO T4 LYSOZYME MUTANT - Y18PHE-METHYLPSEUDO T4 LYSOZYME MUTANT - Y18PHE-METHYL
Structural highlights
FunctionENLYS_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] Publication Abstract from PubMedThe structures and stabilities of proteins are defined by a series of weak non-covalent electrostatic, van der Waals, and hydrogen bond (HB) interactions. In this study, we have designed and engineered halogen bonds (XBs) site-specifically in order to study their structure-energy relationship in a model protein, T4 lysozyme. The evidence for XBs is the displacement of the aromatic side chain towards an oxygen acceptor, at distances that are at or less than the sums of their respective van der Waals radii, when the hydroxyl substituent of the wildtype tyrosine is replaced by an iodine. In addition, thermal melting studies show that the iodine XB rescues the stabilization energy from an otherwise destabilizing substitution (at an equivalent non-interacting site), indicating that the interaction is also present in solution. Quantum chemical calculations show that the XB complements an HB at this site and that solvent structure must also be considered in trying to design molecular interactions such as XBs into biological systems. A bromine substitution also shows displacement of the side chain, but the distances and geometries do not indicate formation of an XB. Thus, we have dissected the contributions from various non-covalent interactions of halogens introduced into proteins, to drive the application of XBs, particularly in biomolecular design. Structure-Energy Relationships of Halogen Bonds in Proteins.,Scholfield MR, Ford MC, Carlsson AC, Butta H, Mehl RA, Ho PS Biochemistry. 2017 Mar 27. doi: 10.1021/acs.biochem.7b00022. PMID:28345933[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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