1npp
From Proteopedia
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| - | [[Image:1npp.jpg|left|200px]] | + | [[Image:1npp.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF AQUIFEX AEOLICUS NUSG IN P2(1)''' | + | {{Structure |
| + | |PDB= 1npp |SIZE=350|CAPTION= <scene name='initialview01'>1npp</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=IPA:ISOPROPYL ALCOHOL'>IPA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= NUSG OR AQ_1931 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 Aquifex aeolicus]) | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF AQUIFEX AEOLICUS NUSG IN P2(1)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NPP is a [ | + | 1NPP 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=1NPP OCA]. |
==Reference== | ==Reference== | ||
| - | A spring-loaded state of NusG in its functional cycle is suggested by X-ray crystallography and supported by site-directed mutants., Knowlton JR, Bubunenko M, Andrykovitch M, Guo W, Routzahn KM, Waugh DS, Court DL, Ji X, Biochemistry. 2003 Mar 4;42(8):2275-81. PMID:[http:// | + | A spring-loaded state of NusG in its functional cycle is suggested by X-ray crystallography and supported by site-directed mutants., Knowlton JR, Bubunenko M, Andrykovitch M, Guo W, Routzahn KM, Waugh DS, Court DL, Ji X, Biochemistry. 2003 Mar 4;42(8):2275-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12600194 12600194] |
[[Category: Aquifex aeolicus]] | [[Category: Aquifex aeolicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rnap transcription factor]] | [[Category: rnap transcription factor]] | ||
| - | ''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 13:00:06 2008'' |
Revision as of 11:00, 20 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | NUSG OR AQ_1931 (Aquifex aeolicus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF AQUIFEX AEOLICUS NUSG IN P2(1)
Overview
Transcription factor NusG is present in all prokaryotes, and orthologous proteins have also been identified in yeast and humans. NusG contains a 27-residue KOW motif, found in ribosomal protein L24 where it interacts with rRNA. NusG in Escherichia coli (EcNusG) is an essential protein and functions as a regulator of Rho-dependent transcription termination, phage lambda N and rRNA transcription antitermination, and phage HK022 Nun termination. Relative to EcNusG, Aquifex aeolicus NusG (AaNusG) and several other bacterial NusG proteins contain a variable insertion sequence of approximately 70 residues in the central region of the molecule. Recently, crystal structures of AaNusG in space groups P2(1) and I222 have been reported; the authors conclude that there are no conserved dimers among the contacting molecules in the crystals [Steiner, T., Kaiser, J. T., Marinkovic, S., Huber, R., and Wahl, M. C. (2002) EMBO J. 21, 4641-4653]. We have independently determined the structures of AaNusG also in two crystal forms, P2(1) and C222(1), and surprisingly found that AaNusG molecules form domain-swapped dimers in both crystals. Additionally, polymerization is also observed in the P2(1) crystal. A unique "ball-and-socket" junction dominates the intermolecular interactions within both oligomers. We believe that this interaction is a clue to the function of the molecule and propose a spring-loaded state in the functional cycle of NusG. The importance of the ball-and-socket junction for the function of NusG is supported by the functional analysis of site-directed mutants.
About this Structure
1NPP is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
Reference
A spring-loaded state of NusG in its functional cycle is suggested by X-ray crystallography and supported by site-directed mutants., Knowlton JR, Bubunenko M, Andrykovitch M, Guo W, Routzahn KM, Waugh DS, Court DL, Ji X, Biochemistry. 2003 Mar 4;42(8):2275-81. PMID:12600194
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