2007
DOI: 10.1002/prot.21270
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Crystal structure of Pyrococcus horikoshii PPC protein at 1.60 Å resolution

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Cited by 11 publications
(10 citation statements)
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“…8). The predicted tertiary structure of the PPC/DUF296 domain of SOB3/AHL29 suggests trimeric oligomerization, which is similar to that observed in seven determined crystal structures of this domain from Bacteria and Archaea [Protein Data Bank (PDB) ID: 2H6L, 2DT4, 2HX0, 2NMU, 2P6Y, 3HTN, and 3HWU] (14,15). Trimer formation in a proposed AHL complex is also supported by the physical interactions observed among AHLs in this study (Figs.…”
Section: Discussionsupporting
confidence: 84%
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“…8). The predicted tertiary structure of the PPC/DUF296 domain of SOB3/AHL29 suggests trimeric oligomerization, which is similar to that observed in seven determined crystal structures of this domain from Bacteria and Archaea [Protein Data Bank (PDB) ID: 2H6L, 2DT4, 2HX0, 2NMU, 2P6Y, 3HTN, and 3HWU] (14,15). Trimer formation in a proposed AHL complex is also supported by the physical interactions observed among AHLs in this study (Figs.…”
Section: Discussionsupporting
confidence: 84%
“…It is also predicted to adopt a similar tertiary structure as observed in the crystal structures of prokaryotic PPC/DUF296 proteins. The PPC/DUF296 proteins form a trimer, where the β-sheets mediate interactions among the three PPC monomers (14). This structure suggests that the PPC/DUF296 domains in Arabidopsis AHL proteins could associate with each other as their counterparts do in prokaryotes.…”
Section: Significancementioning
confidence: 96%
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“…JK974195, a putative DNA-binding protein, belongs to the DUF296 superfamily with unknown function. The AT-hook motif was found in JK974195, which suggested a role in DNA-binding for the protein as a whole [31] (Fig. S2B).…”
Section: Discussionmentioning
confidence: 98%