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PDBsum entry 1rwi
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Sensor domain of the mycobacterium tuberculosis receptor ser/thr protein kinase, Pknd, Forms a highly symmetric beta propeller.
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Authors
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M.C.Good,
A.E.Greenstein,
T.A.Young,
H.L.Ng,
T.Alber.
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Ref.
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J Mol Biol, 2004,
339,
459-469.
[DOI no: ]
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PubMed id
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Abstract
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Diverse pathogenic bacteria produce transmembrane receptor Ser/Thr protein
kinases (STPKs), but little is known about the signals mediated by these
"eukaryotic-like" proteins. To explore the basis for signaling in the
bacterial STPK receptor family, we determined the structure of the sensor domain
of Mycobacterium tuberculosis PknD. In two crystal forms, the PknD sensor domain
forms a rigid, six-bladed beta-propeller with a flexible tether to the
transmembrane domain. The PknD sensor domain is the most symmetric
beta-propeller structure described. All residues that vary most among the blade
subdomains cluster in the large "cup" motif, analogous to the
ligand-binding surface in many beta-propeller proteins. These results suggest
that PknD binds a multivalent ligand that signals by changing the quaternary
structure of the intracellular kinase domain.
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Figure 1.
Figure 1. Crystal structure of the extracellular domain of
PknD. (A) Stereo view of the electron density map (2F[o] -F[c])
of monoclinic crystal form. Electron density is displayed
surrounding one of the invariant prolines in the "cup" and the
exposed Tyr511. (B) The PknD sensor domain forms a six-bladed b
propeller. Four strands constitute each of the six blades. The
numbers around the periphery indicate the blade number, with the
full blade nearest the N terminus labeled 1. The "latch" formed
by the N and C termini is boxed. The 3-4 loop in blade 1 is
disordered. The b propeller forms an approximate cylinder with a
radius of 40 Å and a height of 35 Å. (C) Electron
density (2F[o] -F[c]) showing rings of ordered water molecules
stacked in the central channel of the PknD b propeller. The
central pseudo-symmetry axis runs vertically through the center
of the rings.
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Figure 2.
Figure 2. Similarity the independent PknD sensor domain
structures. The two monomers from the monoclinic crystal form
(P2[1], light blue and dark blue) and the model from the
orthorhombic form (P2[1]2[1]2[1], red) were superimposed. The
C^a rmsd between the three monomers ranged from 0.35-0.52
Å. The high similarity between the three models and the
disorder of the N-terminal 11 residues (dots) implies that the
PknD sensor domain forms a rigid framework that is flexibly
tethered to the predicted transmembrane helix.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2004,
339,
459-469)
copyright 2004.
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