View source for 6akv


==Crystal structure of LysB4, the endolysin from Bacillus cereus-targeting bacteriophage B4==
<StructureSection load='6akv' size='340' side='right'caption='[[6akv]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6akv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_phage_B4 Bacillus phage B4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AKV 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]] 2.4&#8491;</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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6akv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6akv OCA], [https://pdbe.org/6akv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6akv RCSB], [https://www.ebi.ac.uk/pdbsum/6akv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6akv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H9NAL3_9CAUD H9NAL3_9CAUD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Endolysins are bacteriophage-derived enzymes that hydrolyze the peptidoglycan of host bacteria. Endolysins are considered to be promising tools for the control of pathogenic bacteria. LysB4 is an endolysin produced by Bacillus cereus-infecting bacteriophage B4, and consists of an N-terminal enzymatic active domain (EAD) and a C-terminal cell wall binding domain (CBD). LysB4 was discovered for the first time as an Lalanoyl-D-glutamate endopeptidase with the ability to breakdown the peptidoglycan among B. cereus-infecting phages. To understand the activity of LysB4 at the molecular level, this study determined the X-ray crystal structure of the LysB4 EAD, using the full-length LysB4 endolysin. The LysB4 EAD has an active site that is typical of LAS-type enzymes, where Zn(2+) is tetrahedrally coordinated by three amino acid residues and one water molecule. Mutational studies identified essential residues that are involved in lytic activity. Based on the structural and biochemical information about LysB4, we suggest a ligand-docking model and a putative endopeptidase mechanism for the LysB4 EAD. These suggestions add insight into the molecular mechanism of the endolysin LysB4 in B. cereus-infecting phages.

Crystal Structure of LysB4, an Endolysin from Bacillus cereus-Targeting Bacteriophage B4.,Hong S, Son B, Ryu S, Ha NC Mol Cells. 2019 Jan 31;42(1):79-86. doi: 10.14348/molcells.2018.0379. Epub 2018, Dec 5. PMID:30518175<ref>PMID:30518175</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6akv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lysin 3D structures|Lysin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus phage B4]]
[[Category: Large Structures]]
[[Category: Ha N-C]]
[[Category: Hong S]]