3MGE
X-ray Structure of Hexameric HIV-1 CA
Summary for 3MGE
| Entry DOI | 10.2210/pdb3mge/pdb |
| Related | 3gv2 3h47 3h4e |
| Descriptor | Capsid protein p24, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | virus capsid, hexamer, engineered disulfide bonds, viral protein |
| Biological source | Human immunodeficiency virus type 1 (HIV-1) |
| Cellular location | Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P12497 |
| Total number of polymer chains | 1 |
| Total formula weight | 25551.35 |
| Authors | Pornillos, O. (deposition date: 2010-04-05, release date: 2010-07-21, Last modification date: 2024-10-09) |
| Primary citation | Pornillos, O.,Ganser-Pornillos, B.K.,Banumathi, S.,Hua, Y.,Yeager, M. Disulfide Bond Stabilization of the Hexameric Capsomer of Human Immunodeficiency Virus. J.Mol.Biol., 401:985-995, 2010 Cited by PubMed Abstract: The human immunodeficiency virus type 1 capsid is modeled as a fullerene cone that is composed of approximately 250 hexamers and 12 pentamers of the viral CA protein. Structures of CA hexamers have been difficult to obtain because the hexamer-stabilizing interactions are inherently weak, and CA tends to spontaneously assemble into capsid-like particles. Here, we describe a two-step biochemical strategy to obtain soluble CA hexamers for crystallization. First, the hexamer was stabilized by engineering disulfide cross-links (either A14C/E45C or A42C/T54C) between the N-terminal domains of adjacent subunits. Second, the cross-linked hexamers were prevented from polymerizing further into hyperstable capsid-like structures by mutations (W184A and M185A) that interfered with dimeric association between the C-terminal domains that link adjacent hexamers. The structures of two different cross-linked CA hexamers were nearly identical, and we combined the non-mutated portions of the structures to generate an atomic resolution model for the native hexamer. This hybrid approach for structure determination should be applicable to other viral capsomers and protein-protein complexes in general. PubMed: 20600115DOI: 10.1016/j.jmb.2010.06.042 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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