Atomic Structure of Bordetella Bacteriophage Reveals a Jellyroll Fold in CementProtein and a Topologically Distinct HK97-like Fold in Major Capsid Protein

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Atomic Structure of Bordetella Bacteriophage Reveals a Jellyroll Fold in CementProtein and a Topologically Distinct HK97-like Fold in Major Capsid Protein is …
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scholarly articleQ13442814

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P356DOI10.1017/S1431927612002218
P932PMC publication ID4156034
P698PubMed publication ID25197259

P2093author name stringXing Zhang
Lei Jin
Z Hong Zhou
Huatao Guo
Ming Xu
Jeffery F Miller
P2860cites workSequence permutations in the molecular evolution of DNA methyltransferasesQ21045389
3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entryQ24615465
The bacteriophage straight phi29 portal motor can package DNA against a large internal forceQ28199328
Topologically linked protein rings in the bacteriophage HK97 capsidQ29615513
Three-dimensional structure of tropism-switching Bordetella bacteriophageQ30493721
Insights into assembly from structural analysis of bacteriophage PRD1.Q43418282
P433issueSuppl 2
P921main subjectbacteriophageQ165028
protein foldingQ847556
P304page(s)72-73
P577publication date2012-07-01
P1433published inMicroscopy and MicroanalysisQ6840043
P1476titleAtomic Structure of Bordetella Bacteriophage Reveals a Jellyroll Fold in CementProtein and a Topologically Distinct HK97-like Fold in Major Capsid Protein
P478volume18

Reverse relations

Q27680922A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5 Å resolutioncites workP2860

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