View source for 4qnl


==Crystal structure of tail fiber protein gp63.1 from E. coli phage G7C==
<StructureSection load='4qnl' size='340' side='right'caption='[[4qnl]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4qnl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_vB_EcoP_G7C Escherichia phage vB_EcoP_G7C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QNL 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]] 2.411&#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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=4qnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qnl OCA], [https://pdbe.org/4qnl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qnl RCSB], [https://www.ebi.ac.uk/pdbsum/4qnl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qnl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G0XNW5_9CAUD G0XNW5_9CAUD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteriophages recognize and bind to their hosts with the help of receptor-binding proteins (RBPs) that emanate from the phage particle in the form of fibers or tailspikes. RBPs show a great variability in their shapes, sizes, and location on the particle. Some RBPs are known to depolymerize surface polysaccharides of the host while others show no enzymatic activity. Here we report that both RBPs of podovirus G7C - tailspikes gp63.1 and gp66 - are essential for infection of its natural host bacterium E. coli 4s that populates the equine intestinal tract. We characterize the structure and function of gp63.1 and show that unlike any previously described RPB, gp63.1 deacetylates surface polysaccharides of E. coli 4s leaving the backbone of the polysaccharide intact. We demonstrate that gp63.1 and gp66 form a stable complex, in which the N-terminal part of gp66 serves as an attachment site for gp63.1 and anchors the gp63.1-gp66 complex to the G7C tail. The esterase domain of gp63.1 as well as domains mediating the gp63.1-gp66 interaction is widespread among all three families of tailed bacteriophages.

Function of bacteriophage G7C esterase tailspike in host cell adsorption.,Prokhorov NS, Riccio C, Zdorovenko EL, Shneider MM, Browning C, Knirel YA, Leiman PG, Letarov AV Mol Microbiol. 2017 Aug;105(3):385-398. doi: 10.1111/mmi.13710. Epub 2017 Jun 19. PMID:28513100<ref>PMID:28513100</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4qnl" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tailspike protein 3D structures|Tailspike protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia phage vB_EcoP_G7C]]
[[Category: Large Structures]]
[[Category: Browning C]]
[[Category: Leiman PG]]
[[Category: Letarov A]]
[[Category: Prokhorov N]]
[[Category: Riccio C]]