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PDBsum entry 3jvv
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Atp binding protein
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PDB id
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3jvv
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References listed in PDB file
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Key reference
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Title
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P. Aeruginosa pilt structures with and without nucleotide reveal a dynamic type IV pilus retraction motor.
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Authors
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A.M.Misic,
K.A.Satyshur,
K.T.Forest.
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Ref.
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J Mol Biol, 2010,
400,
1011-1021.
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PubMed id
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Abstract
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Type IV pili are bacterial extracellular filaments that can be retracted to
create force and motility. Retraction is accomplished by the motor protein PilT.
Crystal structures of Pseudomonas aeruginosa PilT with and without bound
beta,gamma-methyleneadenosine-5'-triphosphate have been solved at 2.6 A and 3.1
A resolution, respectively, revealing an interlocking hexamer formed by the
action of a crystallographic 2-fold symmetry operator on three subunits in the
asymmetric unit and held together by extensive ionic interactions. The roles of
two invariant carboxylates, Asp Box motif Glu163 and Walker B motif Glu204, have
been assigned to Mg(2+) binding and catalysis, respectively. The nucleotide
ligands in each of the subunits in the asymmetric unit of the
beta,gamma-methyleneadenosine-5'-triphosphate-bound PilT are not equally well
ordered. Similarly, the three subunits in the asymmetric unit of both structures
exhibit differing relative conformations of the two domains. The 12 degrees and
20 degrees domain rotations indicate motions that occur during the ATP-coupled
mechanism of the disassembly of pili into membrane-localized pilin monomers.
Integrating these observations, we propose a three-state "Ready, Active,
Release" model for the action of PilT.
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