1w4a: Difference between revisions
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== | ==P4 protein from PHI12 in complex with AMPcPP and Mn== | ||
Many viruses package their genome into preformed capsids using packaging | <StructureSection load='1w4a' size='340' side='right'caption='[[1w4a]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1w4a]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_phage_phi12 Pseudomonas phage phi12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W4A 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]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=1w4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w4a OCA], [https://pdbe.org/1w4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w4a RCSB], [https://www.ebi.ac.uk/pdbsum/1w4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w4a ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q94M05_9VIRU Q94M05_9VIRU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Many viruses package their genome into preformed capsids using packaging motors powered by the hydrolysis of ATP. The hexameric ATPase P4 of dsRNA bacteriophage phi12, located at the vertices of the icosahedral capsid, is such a packaging motor. We have captured crystallographic structures of P4 for all the key points along the catalytic pathway, including apo, substrate analog bound, and product bound. Substrate and product binding have been observed as both binary complexes and ternary complexes with divalent cations. These structures reveal large movements of the putative RNA binding loop, which are coupled with nucleotide binding and hydrolysis, indicating how ATP hydrolysis drives RNA translocation through cooperative conformational changes. Two distinct conformations of bound nucleotide triphosphate suggest how hydrolysis is activated by RNA binding. This provides a model for chemomechanical coupling for a prototype of the large family of hexameric helicases and oligonucleotide translocating enzymes. | |||
Atomic snapshots of an RNA packaging motor reveal conformational changes linking ATP hydrolysis to RNA translocation.,Mancini EJ, Kainov DE, Grimes JM, Tuma R, Bamford DH, Stuart DI Cell. 2004 Sep 17;118(6):743-55. PMID:15369673<ref>PMID:15369673</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1w4a" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas phage phi12]] | [[Category: Pseudomonas phage phi12]] | ||
[[Category: Bamford DH]] | |||
[[Category: Bamford | [[Category: Grimes JM]] | ||
[[Category: Grimes | [[Category: Kainov DE]] | ||
[[Category: Kainov | [[Category: Mancini EJ]] | ||
[[Category: Mancini | [[Category: Stuart DI]] | ||
[[Category: Stuart | [[Category: Tuma R]] | ||
[[Category: Tuma | |||
Latest revision as of 12:11, 9 May 2024
P4 protein from PHI12 in complex with AMPcPP and MnP4 protein from PHI12 in complex with AMPcPP and Mn
Structural highlights
FunctionPublication Abstract from PubMedMany viruses package their genome into preformed capsids using packaging motors powered by the hydrolysis of ATP. The hexameric ATPase P4 of dsRNA bacteriophage phi12, located at the vertices of the icosahedral capsid, is such a packaging motor. We have captured crystallographic structures of P4 for all the key points along the catalytic pathway, including apo, substrate analog bound, and product bound. Substrate and product binding have been observed as both binary complexes and ternary complexes with divalent cations. These structures reveal large movements of the putative RNA binding loop, which are coupled with nucleotide binding and hydrolysis, indicating how ATP hydrolysis drives RNA translocation through cooperative conformational changes. Two distinct conformations of bound nucleotide triphosphate suggest how hydrolysis is activated by RNA binding. This provides a model for chemomechanical coupling for a prototype of the large family of hexameric helicases and oligonucleotide translocating enzymes. Atomic snapshots of an RNA packaging motor reveal conformational changes linking ATP hydrolysis to RNA translocation.,Mancini EJ, Kainov DE, Grimes JM, Tuma R, Bamford DH, Stuart DI Cell. 2004 Sep 17;118(6):743-55. PMID:15369673[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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