View source for 7esq


==Structure and mutation analysis of the hexameric P4 from Pseudomonas aeruginosa phage phiYY==
<StructureSection load='7esq' size='340' side='right'caption='[[7esq]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7esq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_phage_phiYY Pseudomonas phage phiYY]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ESQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ESQ 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PPV:PYROPHOSPHATE'>PPV</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=7esq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7esq OCA], [https://pdbe.org/7esq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7esq RCSB], [https://www.ebi.ac.uk/pdbsum/7esq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7esq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1U9AK63_9VIRU A0A1U9AK63_9VIRU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
phiYY is a foremost member of Cystoviridae isolated from Pseudomonas aeruginosa. Its P4 protein with NTPase activity is a molecular motor for their genome packing during viral particle assembly. Previously studies on the P4 from four Pseudomonas phages phi6, phi8, phi12 and phi13 reveal that despite of belonging to the same protein family, they are unique in sequence, structure and biochemical properties. To better understand the structure and function of phiYY P4, four crystal structures of phiYY P4 in apo-form or combined with different ligands were solved at the resolution between 1.85 A and 2.43 A, which showed drastic conformation change of the H1 motif in ligand-bound forms compared with in apo-form, a four residue-mutation at the ligand binding pocket abolished its ATPase activity. Furthermore, the truncation mutation of the 50 residues at the C-terminal did not impair the hexamerization and ATP hydrolysis.

Structure and mutation analysis of the hexameric P4 from Pseudomonas aeruginosa phage phiYY.,Zhang C, Li Y, Samad A, Zheng P, Ji Z, Chen F, Zhang H, Jin T Int J Biol Macromol. 2022 Jan 1;194:42-49. doi: 10.1016/j.ijbiomac.2021.11.129., Epub 2021 Nov 29. PMID:34856215<ref>PMID:34856215</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7esq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas phage phiYY]]
[[Category: Jin TC]]
[[Category: Zhang CY]]