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| | ==SOLUTION STRUCTURE OF THE MU NER PROTEIN BY MULTIDIMENSIONAL NMR== | | ==SOLUTION STRUCTURE OF THE MU NER PROTEIN BY MULTIDIMENSIONAL NMR== |
| - | <StructureSection load='1neq' size='340' side='right'caption='[[1neq]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1neq' size='340' side='right'caption='[[1neq]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1neq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_mu Enterobacteria phage mu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NEQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1neq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Mu Escherichia virus Mu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NEQ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ner|1ner]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1neq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1neq OCA], [http://pdbe.org/1neq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1neq RCSB], [http://www.ebi.ac.uk/pdbsum/1neq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1neq ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1neq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1neq OCA], [https://pdbe.org/1neq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1neq RCSB], [https://www.ebi.ac.uk/pdbsum/1neq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1neq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NER_BPMU NER_BPMU]] Negative regulator of transcription starting from the Pe and Pc promoters of Mu. Also negatively regulates its own gene transcription. | + | [https://www.uniprot.org/uniprot/NER_BPMU NER_BPMU] Negative regulator of transcription starting from the Pe and Pc promoters of Mu. Also negatively regulates its own gene transcription. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Enterobacteria phage mu]] | + | [[Category: Escherichia virus Mu]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Clore, G M]] | + | [[Category: Clore GM]] |
| - | [[Category: Gronenborn, A M]] | + | [[Category: Gronenborn AM]] |
| - | [[Category: Strzelecka, T E]] | + | [[Category: Strzelecka TE]] |
| - | [[Category: Dna-binding protein]]
| + | |
| Structural highlights
Function
NER_BPMU Negative regulator of transcription starting from the Pe and Pc promoters of Mu. Also negatively regulates its own gene transcription.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
BACKGROUND: The Mu Ner protein is a small (74 amino acids), basic, DNA-binding protein found in phage Mu. It belongs to a class of proteins, the cro and repressor proteins, that regulate the switch from the lysogenic to the lytic state of the phage life cycle. There is no significant sequence identity between Mu Ner and the cro proteins of other phages, despite their functional similarity. In addition, there is no significant sequence identity with any other DNA-binding proteins, with the exception of Ner from the related phage D108 and the Nlp protein of Escherichia coli. As the tertiary structures of Mu Ner and these two related proteins are unknown, it is clear that a three-dimensional (3D) structure of Mu Ner is essential in order to gain insight into its mode of DNA binding. RESULTS: The 3D solution structure of Mu Ner has been solved by 3D and 4D heteronuclear magnetic resonance spectroscopy. The structure consists of five alpha helices, two of which comprise a helix-turn-helix (HTH) motif. Analysis of line broadening and disappearance of crosspeaks in a 1H-15N correlation spectrum of the Mu Ner-DNA complex suggests that residues in these two helices are most likely to be in contact with the DNA. CONCLUSIONS: Like the functionally analogous cro proteins from phages lambda and 434, the Mu Ner protein possesses a HTH DNA recognition motif. The Ner protein from phage D108 and the Nlp protein from E. coli are likely to have very similar tertiary structures due to high amino-acid-sequence identity with Mu Ner.
The solution structure of the Mu Ner protein reveals a helix-turn-helix DNA recognition motif.,Strzelecka TE, Clore GM, Gronenborn AM Structure. 1995 Oct 15;3(10):1087-95. PMID:8590003[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Strzelecka TE, Clore GM, Gronenborn AM. The solution structure of the Mu Ner protein reveals a helix-turn-helix DNA recognition motif. Structure. 1995 Oct 15;3(10):1087-95. PMID:8590003
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