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The crystal structure of YddB reveals structural homology to FusA, implying conserved function in protein import.

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posted on 2019-10-15, 17:25 authored by Rhys Grinter, Pok Man Leung, Lakshmi C. Wijeyewickrema, Dene Littler, Simone Beckham, Robert N. Pike, Daniel Walker, Chris Greening, Trevor Lithgow

(A) A cartoon representation of YddB (top) and FusA (bottom) showing structural homology between the two proteins despite limited (24%) sequence identity. (B) Dissection of the eleven extracellular loops of YddB (top) and FusA (bottom), showing that they conform to similar length and structural patterns. (C) A stereo view of the extracellular binding pocket of YddB (top = cartoon, bottom = green surface) showing that it consists of a large cavity capable of binding a small globular protein, in common with FusA. (D) Surface/cartoon representation of YddB (top), showing its extracellular binding pocket can accommodate a globular molecule ~28 Å in diameter. The structure of FusA docked with its ferredoxin substrate (bottom) is shown for reference.

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