1m1h
From Proteopedia
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- | [[Image:1m1h.jpg|left|200px]] | + | [[Image:1m1h.jpg|left|200px]] |
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- | '''Crystal structure of Aquifex aeolicus N-utilization substance G (NusG), Space group I222''' | + | {{Structure |
+ | |PDB= 1m1h |SIZE=350|CAPTION= <scene name='initialview01'>1m1h</scene>, resolution 1.95Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of Aquifex aeolicus N-utilization substance G (NusG), Space group I222''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1M1H is a [ | + | 1M1H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1H OCA]. |
==Reference== | ==Reference== | ||
- | Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities., Steiner T, Kaiser JT, Marinkovic S, Huber R, Wahl MC, EMBO J. 2002 Sep 2;21(17):4641-53. PMID:[http:// | + | Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities., Steiner T, Kaiser JT, Marinkovic S, Huber R, Wahl MC, EMBO J. 2002 Sep 2;21(17):4641-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12198166 12198166] |
[[Category: Aquifex aeolicus]] | [[Category: Aquifex aeolicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription termination]] | [[Category: transcription termination]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:37:44 2008'' |
Revision as of 10:37, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of Aquifex aeolicus N-utilization substance G (NusG), Space group I222
Overview
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.
About this Structure
1M1H is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
Reference
Crystal structures of transcription factor NusG in light of its nucleic acid- and protein-binding activities., Steiner T, Kaiser JT, Marinkovic S, Huber R, Wahl MC, EMBO J. 2002 Sep 2;21(17):4641-53. PMID:12198166
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