2q9e: Difference between revisions
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==Structure of spin-labeled T4 lysozyme mutant S44R1== | ==Structure of spin-labeled T4 lysozyme mutant S44R1== | ||
<StructureSection load='2q9e' size='340' side='right' caption='[[2q9e]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2q9e' size='340' side='right' caption='[[2q9e]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</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='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=2q9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q9e OCA], [http://pdbe.org/2q9e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q9e RCSB], [http://www.ebi.ac.uk/pdbsum/2q9e 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=2q9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q9e OCA], [http://pdbe.org/2q9e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q9e RCSB], [http://www.ebi.ac.uk/pdbsum/2q9e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2q9e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
Revision as of 12:41, 18 October 2017
Structure of spin-labeled T4 lysozyme mutant S44R1Structure of spin-labeled T4 lysozyme mutant S44R1
Structural highlights
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 PubMedSite-directed spin labeling provides a means for exploring structure and dynamics in proteins. To interpret the complex EPR spectra that often arise, it is necessary to characterize the rotamers of the spin-labeled side chain and the interactions they make with the local environment in proteins of known structure. For this purpose, crystal structures have been determined for T4 lysozyme bearing a nitroxide side chain (R1) at the solvent-exposed helical sites 41 and 44 in the B helix. These sites are of particular interest in that the corresponding EPR spectra reveal two dynamic states of R1, one of which is relatively immobilized suggesting interactions of the nitroxide with the environment. The crystal structures together with the effect of mutagenesis of nearest neighbors on the motion of R1 suggest intrahelical interactions of 41R1 with the i + 4 residue and of 44R1 with the i + 1 residue. Such interactions appear to be specific to particular rotamers of the R1 side chain. Structural determinants of nitroxide motion in spin-labeled proteins: solvent-exposed sites in helix B of T4 lysozyme.,Guo Z, Cascio D, Hideg K, Hubbell WL Protein Sci. 2008 Feb;17(2):228-39. Epub 2007 Dec 20. PMID:18096642[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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