2GQQ
Crystal Structure of E. coli Leucine-responsive regulatory protein (Lrp)
Summary for 2GQQ
| Entry DOI | 10.2210/pdb2gqq/pdb |
| Descriptor | Leucine-responsive regulatory protein (1 entity in total) |
| Functional Keywords | helix-turn-helix, transcription |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 75134.40 |
| Authors | de los Rios, S.,Perona, J.J. (deposition date: 2006-04-21, release date: 2007-03-06, Last modification date: 2024-02-14) |
| Primary citation | de Los Rios, S.,Perona, J.J. Structure of the Escherichia coli Leucine-responsive Regulatory Protein Lrp Reveals a Novel Octameric Assembly. J.Mol.Biol., 366:1589-1602, 2007 Cited by PubMed Abstract: The structure of Escherichia coli leucine-responsive regulatory protein (Lrp) co-crystallized with a short duplex oligodeoxynucleotide reveals a novel quaternary assembly in which the protein octamer forms an open, linear array of four dimers. In contrast, structures of the Lrp homologs LrpA, LrpC and AsnC crystallized in the absence of DNA show that these proteins instead form highly symmetrical octamers in which the four dimers form a closed ring. Although the DNA is disordered within the Lrp crystal, comparative analyses suggest that the observed differences in quaternary state may arise from DNA interactions during crystallization. Interconversion of these conformations, possibly in response to DNA or leucine binding, provides an underlying mechanism to alter the relative spatial orientation of the DNA-binding domains. Breaking of the closed octamer symmetry may be a common essential step in the formation of active DNA complexes by all members of the Lrp/AsnC family of transcriptional regulatory proteins. PubMed: 17223133DOI: 10.1016/j.jmb.2006.12.032 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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