5jgx
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==Spin-Labeled T4 Lysozyme Construct V131V1== | ==Spin-Labeled T4 Lysozyme Construct V131V1== | ||
| - | <StructureSection load='5jgx' size='340' side='right' caption='[[5jgx]], [[Resolution|resolution]] 1.53Å' scene=''> | + | <StructureSection load='5jgx' size='340' side='right'caption='[[5jgx]], [[Resolution|resolution]] 1.53Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5jgx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JGX OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5jgx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_T4 Escherichia phage T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JGX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=V1A:S-(1-OXYL-2,2,5,5-TETRAMETHYL-2,5-DIHYDRO-1H-IMIDAZOL-4-YL)+METHANESULFONOTHIOATE'>V1A</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.533Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=V1A:S-(1-OXYL-2,2,5,5-TETRAMETHYL-2,5-DIHYDRO-1H-IMIDAZOL-4-YL)+METHANESULFONOTHIOATE'>V1A</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=5jgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jgx OCA], [https://pdbe.org/5jgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jgx RCSB], [https://www.ebi.ac.uk/pdbsum/5jgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jgx ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== 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> |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pulsed electron paramagnetic resonance experiments can measure individual distances between two spin-labeled side chains in proteins in the range of approximately 1.5-8 nm. However, the flexibility of traditional spin-labeled side chains leads to diffuse spin density loci and thus distance distributions with relatively broad peaks, thereby complicating the interpretation of protein conformational states. Here we analyzed the spin-labeled V1 side chain, which is internally anchored and hence less flexible. Crystal structures of V1-labeled T4 lysozyme constructs carrying the V1 side chain on alpha-helical segments suggest that V1 side chains adopt only a few discrete rotamers. In most cases, only one rotamer is observed at a given site, explaining the frequently observed narrow distance distribution for doubly V1-labeled proteins. We used the present data to derive guidelines that may allow distance interpretation of other V1-labeled proteins for higher-precision structural modeling. | ||
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| + | Toward Precise Interpretation of DEER-Based Distance Distributions: Insights from Structural Characterization of V1 Spin-Labeled Side Chains.,Balo AR, Feyrer H, Ernst OP Biochemistry. 2016 Sep 20;55(37):5256-63. doi: 10.1021/acs.biochem.6b00608. Epub , 2016 Sep 2. PMID:27532325<ref>PMID:27532325</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5jgx" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Lysin 3D structures|Lysin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia phage T4]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Balo AR]] |
| - | [[Category: | + | [[Category: Ernst OP]] |
| - | [[Category: | + | [[Category: Feyrer H]] |
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Current revision
Spin-Labeled T4 Lysozyme Construct V131V1
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