Biological Nitrogen Fixation 2015
DOI: 10.1002/9781119053095.ch13
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How Does the DraG–P II Complex Regulate Nitrogenase Activity in Azospirillum brasilense?

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(2 citation statements)
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“…In contrast to all known structures of PII proteins complexed to their targets, the interaction of DraG with GlnZ does not require the GlnZ T‐loop. Although the GlnZ T‐loop is highly flexible and could not be modeled in the previously determined DraG‐GlnZ crystal structure , the interaction with DraG is expected to restrict the mobility of the T‐loop, as more conformations will be forbidden within the DraG‐GlnZ . This mode of interaction allows DraG and GlnZ to form a complex with AmtB, in which the GlnZ T‐loops participate and become ordered, by analogy with the AmtB‐GlnK complex .…”
Section: Resultsmentioning
confidence: 99%
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“…In contrast to all known structures of PII proteins complexed to their targets, the interaction of DraG with GlnZ does not require the GlnZ T‐loop. Although the GlnZ T‐loop is highly flexible and could not be modeled in the previously determined DraG‐GlnZ crystal structure , the interaction with DraG is expected to restrict the mobility of the T‐loop, as more conformations will be forbidden within the DraG‐GlnZ . This mode of interaction allows DraG and GlnZ to form a complex with AmtB, in which the GlnZ T‐loops participate and become ordered, by analogy with the AmtB‐GlnK complex .…”
Section: Resultsmentioning
confidence: 99%
“…Our current hypothesis is that the DraG-GlnZ complex is not stable enough in vivo to effectively inhibit DraG. The further engagement of AmtB to form a ternary DraG-GlnZ-AmtB complex would be required to enhance the apparent affinity of the DraG-GlnZ interaction thereby allowing effective inhibition of DraG [17,18,20].…”
Section: Discussionmentioning
confidence: 99%