Crystal structure of the potassium-

importing
KdpFABC membrane complex
AND ALL OF ITS POTASSIUM-IMPORTING GLORY
structure at 2.9 A resolution using
experimental phases based on a Hg
derivative
The asymmetric unit consists of
three copies of the KdpFABC
complex, which each appear to
have the same conformation
Structure

 Total Structure Weight: 465934.03 Da

 Atom Count: 32663
 Residue Count: 4335
 Unique protein chains: 4
 Method: X-RAY DIFFRACTION
 Resolution: 2.9 Å
Background

 In E.coli K+ is involved in many functions such as:

 pH homeostasis
 Turgor maintenance
 And enzyme activation
 There are many different ways that these cells handle potassium
transport
 kdpFABC is a high affinity ATP-driven K+ scavenging system
 Synthesis occurs when external K+ levels reach below 100 μm
Function

 The function of the KdpFABC complex is to pump potassium ions

across the membrane
 KdpFABC is unique in that is consists of four subunits and each
subunit has a specific function
 It is classified as P-type ATPase
 KdpFABC is a cross between a potassium pump and a potassium
channel
 Functions are interesting because they are on separate
polypeptides
 Spatial separation of ion transport is done by KdpA (channel like)
 ATP hydrolysis is done by KdpB (pump like)
A simplified view of the complex
Mechanism
KdpA
Intramembrane tunnel provides a possible proton wire for introducing
charge into that site in response to K+ binding to the selectivity filter of
KdpA
KdpB
ATP + H2O + K+(Out) = ADP + phosphate + K+(In)
Coupling of KdpA & KdpB

 On the one hand, the presence or absence of K+ in KdpA should

initiate autophosphorylation of Asp307 in KdpB
 conformational change in KdpB should control gating of ion sites in
KdpA.
 The latter step is likely to involve the kinked helix from the distal part of
the D3M2 element of KdpA, which forms a strong interaction with the P
domain of KdpB involving a salt bridge between Arg400 from KdpA and
Asp300 and Asp302 from KdpB
ATP Binding
References

 https://phys.org/news/2017-06-insight-central-biological-dogma-
ion.html
 Huang, Ching-Shin, Bjørn Panyella Pedersen, and David L. Stokes.
"Crystal structure of the potassium-importing KdpFABC membrane
complex." Nature 546.7660 (2017): 681.