Mark Hilge
Structural Biology
Gallery
Movies
Na+/K+ ATPase
N-domain
Rotation of the 25kD nucleotide binding domain of the Na+/K+
ATPase in complex with ATP.
QuickTime Movie 270 x 300 Pixel
DOWNLOAD N-domain.mov 1,7 MB
11Å EM structure
Glas body representation based on the EM map of the 11Å
structure of the Na+/K+ ATPase fitted with the N-domain
structure (red) determined by NMR and the X-ray structure of
the A-, P-, and transmembrane domain (yellow) of the Ca2+
ATPase. The EM map was kindly rovided by Bill Rice & coworkers.
QuickTime Movie 330 x 450 Pixel
DOWNLOAD rotation3.mov 860 KB
Pump cycle
Molecular movie of the entire reaction cycle of the Na+/K+
ATPase. A detailed description can be found here.
QuickTime Movie 400 x 384 Pixel
DOWNLOAD pump-cycle-medium.mov 11,9 MB
Na+/Ca2+ exchanger
Hypothetical model
Rotation of the hypothetical Na+/Ca2+ exchanger model that
consists of a transmembrane domain (yellow), containing the
Na+ and Ca2+ transport sites, and three regulatory domains
located in the cytosol. Domains in red and green represent
CBD1 and CBD2, respectively. Ca2+ binding and release events
are relayed via the CLD (blue) to the ion-transport sites within
the transmembrane domain.
QuickTime Movie 500 x 600 Pixel
DOWNLOAD rot.-NCX.mov 3,7 MB
Binding of Ca2+
to CBD1 and CBD2
CBD1 is in red, CBD2 in green. Regions that undergo substantial
conformational changes upon binding and release of Ca2+ are
colored yellow and orange. From our NMR data we know that
CBD1 Ca2+ binding sites in the absence of Ca2+ are largely
unstructured. As the primary Ca2+ sensor CBD1 binds Ca2+ ions
with affinities of around 100-400 nM. In contrast, conformational
changes in CBD2 are relatively minor.
QuickTime Movie 334 x 400 Pixel
DOWNLOAD H1+H2.mov 4,3 MB Covers
Molecular Cell
22 (1), 2006
Major players in Ca2+ homeostasis involve the Na+/Ca2+
exchanger, the plasma membrane and endoplasmic reticulum
Ca2+ ATPases, the L-type Ca2+ channel DHPR as well as the
ryanodine and IP3 receptors in the endoplasmic reticulum.
With the exception of the Na+/Ca2+ exchanger all depicted
transporters are either based on X-ray, NMR or EM structures.
The mitochondrial Ca2+ uniporter and the mitochondrial Na+/Ca2+
exchanger are omitted due to lack of structural information.
Artwork was created by Stephan Hilge.
Ann N Y Acad Sci. Volume 1099, 2007
Hypothetical model of the two major Ca2+ export systems, the
Na+/Ca2+ exchanger (NCX) and the plasma membrane Ca2+
ATPase (PMCA). Artwork was created by Stephan Hilge.
Reprints
b-Mannanase
Hilge M, Gloor SM, Rypniewski W, Sauer O, Heightman TD,
Zimmermann W, Winterhalter K, Piontek K. High-
resolution native and complex structures of thermostable
b-mannanase from Thermomonospora fusca – substrate
specificity in glycosyl hydrolase family 5. Structure 6,
1433-44 (1998).
DOWNLOAD Structure.pdf 1 MB
Na+/K+ ATPase
Hilge M, Siegal G, Vuister GW, Güntert P, Gloor SM,
Abrahams JP. ATP-induced conformational changes of
the nucleotide-binding domain of Na,K-ATPase. Nat Struct
Biol. 10, 468-74 (2003).
DOWNLOAD NSB.pdf 1,5 MB
Na+/Ca2+ exchanger
Hilge M, Aelen J, Vuister GW. Ca2+ regulation in the
Na+/Ca2+ exchanger involves two markedly different
Ca2+ sensors. Mol Cell. 22, 15-25 (2006).
DOWNLOAD MC.pdf 828kB
Hilge M, Aelen J, Perrakis A, Vuister GW.
Structural basis
for Ca2+ regulation in the Na+/Ca2+ exchanger. Ann N Y
Acad Sci. 1099, 7-15 (2007).
DOWNLOAD NYAS.pdf 5,4 MB
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