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| {{STRUCTURE_1m1g| PDB=1m1g | SCENE= }} | | {{STRUCTURE_1m1g| PDB=1m1g | SCENE= }} |
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| '''Crystal Structure of Aquifex aeolicus N-utilization substance G (NusG), Space Group P2(1)'''
| | ===Crystal Structure of Aquifex aeolicus N-utilization substance G (NusG), Space Group P2(1)=== |
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| ==Overview==
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| Microbial transcription modulator NusG interacts with RNA polymerase and termination factor rho, displaying striking functional homology to eukaryotic Spt5. The protein is also a translational regulator. We have determined crystal structures of Aquifex aeolicus NusG showing a modular design: an N-terminal RNP-like domain, a C-terminal element with a KOW sequence motif and a species-specific immunoglobulin-like fold. The structures reveal bona fide nucleic acid binding sites, and nucleic acid binding activities can be detected for NusG from three organisms and for the KOW element alone. A conserved KOW domain is defined as a new class of nucleic acid binding folds. This module is a close structural homolog of tudor protein-protein interaction motifs. Putative protein binding sites for the RNP and KOW domains can be deduced, which differ from the areas implicated in nucleic acid interactions. The results strongly argue that both protein and nucleic acid contacts are important for NusG's functions and that the factor can act as an adaptor mediating indirect protein-nucleic acid associations.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12198166}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12198166 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12198166}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Rnp motif]] | | [[Category: Rnp motif]] |
| [[Category: Transcription termination]] | | [[Category: Transcription termination]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:31:04 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:00:41 2008'' |