1MML
MECHANISTIC IMPLICATIONS FROM THE STRUCTURE OF A CATALYTIC FRAGMENT OF MMLV REVERSE TRANSCRIPTASE
Summary for 1MML
| Entry DOI | 10.2210/pdb1mml/pdb |
| Descriptor | MMLV REVERSE TRANSCRIPTASE (2 entities in total) |
| Functional Keywords | reverse transcriptase |
| Biological source | Moloney murine leukemia virus |
| Cellular location | Gag-Pol polyprotein: Host cell membrane; Lipid-anchor (Potential). Matrix protein p15: Virion (Potential). Capsid protein p30: Virion (Potential). Nucleocapsid protein p10: Virion (Potential): P03355 |
| Total number of polymer chains | 1 |
| Total formula weight | 29945.38 |
| Authors | Georgiadis, M.M.,Jessen, S.M.,Ogata, C.M.,Telesnitsky, A.,Goff, S.P.,Hendrickson, W.A. (deposition date: 1995-07-18, release date: 1995-10-15, Last modification date: 2024-02-14) |
| Primary citation | Georgiadis, M.M.,Jessen, S.M.,Ogata, C.M.,Telesnitsky, A.,Goff, S.P.,Hendrickson, W.A. Mechanistic implications from the structure of a catalytic fragment of Moloney murine leukemia virus reverse transcriptase. Structure, 3:879-892, 1995 Cited by PubMed Abstract: Reverse transcriptase (RT) converts the single-stranded RNA genome of a retrovirus into a double-stranded DNA copy for integration into the host genome. This process requires ribonuclease H as well as RNA- and DNA-directed DNA polymerase activities. Although the overall organization of HIV-1 RT is known from previously reported crystal structures, no structure of a complex including a metal ion, which is essential for its catalytic activity, has been reported. PubMed: 8535782DOI: 10.1016/S0969-2126(01)00223-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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