5jwt
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==T4 Lysozyme L99A/M102Q with Benzene Bound== | |
| + | <StructureSection load='5jwt' size='340' side='right' caption='[[5jwt]], [[Resolution|resolution]] 1.41Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5jwt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JWT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JWT FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNZ:BENZENE'>BNZ</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jwu|5jwu]], [[5jwv|5jwv]], [[5jww|5jww]], [[5jwx|5jwx]], [[5jws|5jws]]</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=5jwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jwt OCA], [http://pdbe.org/5jwt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jwt RCSB], [http://www.ebi.ac.uk/pdbsum/5jwt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jwt ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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 == | ||
| + | Protein crystallography and calorimetry were used to characterize the binding of 1,2-azaborines to model cavities in T4 lysozyme in direct comparison to their carbonaceous counterparts. In the apolar L99A cavity, affinity for Ab dropped only slightly versus benzene. In the cavity designed to accommodate a single hydrogen bond (L99A/M102Q), Gln102 horizontal lineO...H-N hydrogen bonding for Ab and BEtAb was observed in the crystallographic complexes. The strength of the hydrogen bonding was estimated as 0.94 and 0.64 kcal/mol for Ab and BEtAb, respectively. This work unambiguously demonstrates that 1,2-azaborines can be readily accommodated in classic aryl recognition pockets and establishes one of 1,2-azaborine's distinguishing features from its carbonaceous isostere benzene: its ability to serve as an NH hydrogen bond donor in a biological setting. | ||
| - | + | Hydrogen Bonding of 1,2-Azaborines in the Binding Cavity of T4 Lysozyme Mutants: Structures and Thermodynamics.,Lee H, Fischer M, Shoichet BK, Liu SY J Am Chem Soc. 2016 Sep 12. PMID:27603116<ref>PMID:27603116</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5jwt" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Lysozyme]] | ||
| + | [[Category: Fischer, M]] | ||
| + | [[Category: Lee, H]] | ||
| + | [[Category: Liu, S Y]] | ||
| + | [[Category: Shoichet, B K]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Phage lysozyme azaborine]] | ||
Revision as of 13:54, 21 September 2016
T4 Lysozyme L99A/M102Q with Benzene Bound
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