5lwo
From Proteopedia
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== Function == | == 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> | [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> | ||
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| - | == Publication Abstract from PubMed == | ||
| - | Site-directed spin labeling is a versatile tool to study structure as well as dynamics of proteins using EPR spectroscopy. Methanethiosulfonate (MTS) spin labels tethered through a disulfide linkage to an engineered cysteine residue were used in a large number of studies to extract structural as well as dynamic information on the protein from the rotational dynamics of the nitroxide moiety. The ring itself was always considered to be a rigid body. In this contribution, we present a combination of high-resolution X-ray crystallography and EPR spectroscopy of spin-labeled protein single crystals demonstrating that the nitroxide ring inverts fast at ambient temperature while exhibiting nonplanar conformations at low temperature. We have used quantum chemical calculations to explore the potential energy that determines the ring dynamics as well as the impact of the geometry on the magnetic parameters probed by EPR spectroscopy. | ||
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| - | Internal Dynamics of the 3-Pyrroline-N-Oxide Ring in Spin-Labeled Proteins.,Consentius P, Loll B, Gohlke U, Alings C, Muller C, Muller R, Teutloff C, Heinemann U, Kaupp M, Wahl MC, Risse T J Phys Chem Lett. 2017 Feb 23:1113-1117. doi: 10.1021/acs.jpclett.6b02971. PMID:28221042<ref>PMID:28221042</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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| - | <div class="pdbe-citations 5lwo" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Structure of Spin-labelled T4 lysozyme mutant L115C-R119C-R1 at 100K
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Categories: Escherichia virus T4 | Large Structures | Consentius P | Gohlke U | Heinemann U | Kaupp M | Loll B | Mueller R | Risse T | Wahl MC
