1npr: Difference between revisions

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[[Image:1npr.gif|left|200px]]<br /><applet load="1npr" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1npr.gif|left|200px]]<br /><applet load="1npr" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1npr, resolution 2.21Å" />

'''CRYSTAL STRUCTURE OF AQUIFEX AEOLICUS NUSG IN C222(1)'''<br />

==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.

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==

1NPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1NPR OCA].

1NPR is a [http://en.wikipedia.org/wiki/Single_protein 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=1NPR OCA].

==Reference==

Line 15:

[[Category: Andrykovitch, M.]]

[[Category: Bubunenko, M.]]

[[Category: Court, D.L.]]

[[Category: Court, D L.]]

[[Category: Guo, W.]]

[[Category: Ji, X.]]

[[Category: Knowlton, J.R.]]

[[Category: Knowlton, J R.]]

[[Category: Routzhan, K.M.]]

[[Category: Routzhan, K M.]]

[[Category: Waugh, D.S.]]

[[Category: Waugh, D S.]]

[[Category: nusg]]

[[Category: transcription factor]]

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@@ Line 1: / Line 1: @@
-[[Image:1npr.gif|left|200px]]<br /><applet load="1npr" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1npr.gif|left|200px]]<br /><applet load="1npr" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1npr, resolution 2.21&Aring;" />
 '''CRYSTAL STRUCTURE OF AQUIFEX AEOLICUS NUSG IN C222(1)'''<br />
 ==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.
+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==
-NPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NPR OCA].
+NPR is a [http://en.wikipedia.org/wiki/Single_protein 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=1NPR OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Andrykovitch, M.]]
 [[Category: Bubunenko, M.]]
-[[Category: Court, D.L.]]
+[[Category: Court, D L.]]
 [[Category: Guo, W.]]
 [[Category: Ji, X.]]
-[[Category: Knowlton, J.R.]]
+[[Category: Knowlton, J R.]]
-[[Category: Routzhan, K.M.]]
+[[Category: Routzhan, K M.]]
-[[Category: Waugh, D.S.]]
+[[Category: Waugh, D S.]]
 [[Category: nusg]]
 [[Category: transcription factor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:28:17 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:43 2008''