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New page: left|200px<br /><applet load="1m1g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m1g, resolution 2.0Å" /> '''Crystal Structure of ... |
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== | ==Crystal Structure of Aquifex aeolicus N-utilization substance G (NusG), Space Group P2(1)== | ||
Microbial transcription modulator NusG interacts with RNA polymerase and | <StructureSection load='1m1g' size='340' side='right'caption='[[1m1g]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1m1g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M1G FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1g OCA], [https://pdbe.org/1m1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m1g RCSB], [https://www.ebi.ac.uk/pdbsum/1m1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m1g ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NUSG_AQUAE NUSG_AQUAE] Influences transcription termination and antitermination. Acts as a component of the transcription complex, and interacts with the termination factor rho and RNA polymerase (By similarity). | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m1/1m1g_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m1g ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:12198166</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1m1g" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aquifex aeolicus]] | [[Category: Aquifex aeolicus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Huber | [[Category: Huber R]] | ||
[[Category: Kaiser | [[Category: Kaiser JT]] | ||
[[Category: Marinkovic | [[Category: Marinkovic S]] | ||
[[Category: Steiner | [[Category: Steiner T]] | ||
[[Category: Wahl | [[Category: Wahl MC]] | ||
Latest revision as of 09:59, 30 October 2024
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)
Structural highlights
FunctionNUSG_AQUAE Influences transcription termination and antitermination. Acts as a component of the transcription complex, and interacts with the termination factor rho and RNA polymerase (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMicrobial 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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