1cr5
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(New page: 200px<br /><applet load="1cr5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cr5, resolution 2.3Å" /> '''N-TERMINAL DOMAIN OF ...)
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Revision as of 10:34, 20 November 2007
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N-TERMINAL DOMAIN OF SEC18P
Overview
Yeast Sec18p and its mammalian orthologue N-ethylmaleimide-sensitive, fusion protein (NSF) are hexameric ATPases with a central role in vesicle, trafficking. Aided by soluble adapter factors (SNAPs), Sec18p/NSF induces, ATP-dependent disassembly of a complex of integral membrane proteins from, the vesicle and target membranes (SNAP receptors). During the ATP, hydrolysis cycle, the Sec18p/NSF homohexamer undergoes a large-scale, conformational change involving repositioning of the most N terminal of, the three domains of each protomer, a domain that is required for, SNAP-mediated interaction with SNAP receptors. Whether an internal, conformational change in the N-terminal domains accompanies their, reorientation with respect to the rest of the hexamer remains to be, addressed. We have determined the structure of the N-terminal domain from, Sec18p by x-ray crystallography. The Sec18p N-terminal domain consists of, two beta-sheet-rich subdomains connected by a short linker. A conserved, basic cleft opposite the linker may constitute a SNAP-binding site., Despite structural variability in the linker region and in an adjacent, loop, all three independent molecules in the crystal asymmetric unit have, the identical subdomain interface, supporting the notion that this, interface is a preferred packing arrangement. However, the linker, flexibility allows for the possibility that other subdomain orientations, may be sampled.
About this Structure
1CR5 is a Single protein structure of sequence from Saccharomyces cerevisiae with NEN as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Sec18p N-terminal domain., Babor SM, Fass D, Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14759-64. PMID:10611286
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