The hexamerization domain of N-ethylmaleimide-sensitive factor: structural clues to chaperone function.
The hexameric structure of the D2 ATP-binding module of N-ethylmaleimide-sensitive factor (NSF), a chaperone involved in SNARE complex disassembly, was recently determined. This structure and the previously determined structure of the DNA polymerase III delta' subunit have far-reaching biological significance because these modules are related to diverse ATPases that promote the assembly, disassembly and operation of various protein complexes.
Neuwald
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AF
Cold Spring Harbor Laboratory, PO Box 1001, Bungtown Road, Cold Spring Harbor, NY 11724, USA. neuwald@cshl.org
D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry*; D008565:Membrane Proteins / Q000378:metabolism; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry*; D008969:Molecular Sequence Data; D052066:N-Ethylmaleimide-Sensitive Proteins; D011487:Protein Conformation; D050600:SNARE Proteins; D016415:Sequence Alignment; D033921:Vesicular Transport Proteins
D002352:Carrier Proteins; D008565:Membrane Proteins; D018832:Molecular Chaperones; D050600:SNARE Proteins; D033921:Vesicular Transport Proteins; D000255:Adenosine Triphosphate; D052066:N-Ethylmaleimide-Sensitive Proteins