1g5g
From Proteopedia
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|PDB= 1g5g |SIZE=350|CAPTION= <scene name='initialview01'>1g5g</scene>, resolution 3.30Å | |PDB= 1g5g |SIZE=350|CAPTION= <scene name='initialview01'>1g5g</scene>, resolution 3.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | + | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g5g OCA], [http://www.ebi.ac.uk/pdbsum/1g5g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g5g RCSB]</span> | ||
}} | }} | ||
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[[Category: Lawrence, M C.]] | [[Category: Lawrence, M C.]] | ||
[[Category: Smith, B J.]] | [[Category: Smith, B J.]] | ||
| - | [[Category: NAG]] | ||
[[Category: fusion protein]] | [[Category: fusion protein]] | ||
[[Category: ndv]] | [[Category: ndv]] | ||
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[[Category: paramyxovirus]] | [[Category: paramyxovirus]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:36:59 2008'' |
Revision as of 17:37, 30 March 2008
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| , resolution 3.30Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FRAGMENT OF FUSION PROTEIN FROM NEWCASTLE DISEASE VIRUS
Overview
BACKGROUND: Membrane fusion within the Paramyxoviridae family of viruses is mediated by a surface glycoprotein termed the "F", or fusion, protein. Membrane fusion is assumed to involve a series of structural transitions of F from a metastable (prefusion) state to a highly stable (postfusion) state. No detail is available at the atomic level regarding the metastable form of these proteins or regarding the transitions accompanying fusion. RESULTS: The three-dimensional structure of the fusion protein of Newcastle disease virus (NDV-F) has been determined. The trimeric NDV-F molecule is organized into head, neck, and stalk regions. The head is comprised of a highly twisted beta domain and an additional immunoglobulin-like beta domain. The neck is formed by the C-terminal extension of the heptad repeat region HR-A, capped by a four-helical bundle. The C terminus of HR-A is encased by a further helix HR-C and a 4-stranded beta sheet. The stalk is formed by the remaining visible portion of HR-A and by polypeptide immediately N-terminal to the C-terminal heptad repeat region HR-B. An axial channel extends through the head and neck and is fenestrated by three large radial channels located approximately at the head-neck interface. CONCLUSION: We propose that prior to fusion activation, the hydrophobic fusion peptides in NDV-F are sequestered within the radial channels within the head, with the central HR-A coiled coil being only partly formed. Fusion activation then involves, inter alia, the assembly of a complete HR-A coiled coil, with the fusion peptides and transmembrane anchors being brought into close proximity. The structure of NDV-F is fundamentally different than that of influenza virus hemagglutinin, in that the central coiled coil is in the opposite orientation with respect to the viral membrane.
About this Structure
1G5G is a Single protein structure of sequence from Newcastle disease virus. Full crystallographic information is available from OCA.
Reference
The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusion., Chen L, Gorman JJ, McKimm-Breschkin J, Lawrence LJ, Tulloch PA, Smith BJ, Colman PM, Lawrence MC, Structure. 2001 Mar 7;9(3):255-66. PMID:11286892
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