1m1h

<StructureSection load='1m1h' size='340' side='right' caption='[[1m1h]], [[Resolution|resolution]] 1.95&Aring;' scene=''>

<table><tr><td colspan='2'>[[1m1h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M1H FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m1g|1m1g]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1h OCA], [http://pdbe.org/1m1h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m1h RCSB], [http://www.ebi.ac.uk/pdbsum/1m1h PDBsum]</span></td></tr>

[[http://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).

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m1/1m1h_consurf.spt"</scriptWhenChecked>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1m1h" style="background-color:#fffaf0;"></div>

==See Also==

*[[RapA%2C a Swi2/Snf2 protein|RapA%2C a Swi2/Snf2 protein]]

== References ==

<references/>

[[Category: Aquifex aeolicus huber and stetter 2001]]

[[Category: Huber, R]]

[[Category: Kaiser, J T]]

[[Category: Marinkovic, S]]

[[Category: Steiner, T]]

[[Category: Wahl, M C]]

[[Category: Transcription termination]]