1npp
From Proteopedia
(New page: 200px<br /><applet load="1npp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1npp, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1npp.jpg|left|200px]]<br /><applet load="1npp" size=" | + | [[Image:1npp.jpg|left|200px]]<br /><applet load="1npp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1npp, resolution 2.00Å" /> | caption="1npp, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF AQUIFEX AEOLICUS NUSG IN P2(1)'''<br /> | '''CRYSTAL STRUCTURE OF AQUIFEX AEOLICUS NUSG IN P2(1)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Transcription factor NusG is present in all prokaryotes, and orthologous | + | 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== | ==About this Structure== | ||
| - | 1NPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with IPA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1NPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NPP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Andrykovitch, M.]] | [[Category: Andrykovitch, M.]] | ||
[[Category: Bubunenko, M.]] | [[Category: Bubunenko, M.]] | ||
| - | [[Category: Court, D | + | [[Category: Court, D L.]] |
[[Category: Guo, W.]] | [[Category: Guo, W.]] | ||
[[Category: Ji, X.]] | [[Category: Ji, X.]] | ||
| - | [[Category: Knowlton, J | + | [[Category: Knowlton, J R.]] |
| - | [[Category: Routzahn, K | + | [[Category: Routzahn, K M.]] |
| - | [[Category: Waugh, D | + | [[Category: Waugh, D S.]] |
[[Category: IPA]] | [[Category: IPA]] | ||
[[Category: nusg]] | [[Category: nusg]] | ||
[[Category: rnap transcription factor]] | [[Category: rnap transcription factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:43 2008'' |
Revision as of 12:08, 21 February 2008
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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 with as ligand. 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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