1hh2: Difference between revisions
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<StructureSection load='1hh2' size='340' side='right'caption='[[1hh2]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1hh2' size='340' side='right'caption='[[1hh2]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hh2]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1hh2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HH2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hh2 OCA], [https://pdbe.org/1hh2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hh2 RCSB], [https://www.ebi.ac.uk/pdbsum/1hh2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hh2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9X298_THEMA Q9X298_THEMA] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bartunik | [[Category: Thermotoga maritima]] | ||
[[Category: Bourenkov | [[Category: Bartunik HD]] | ||
[[Category: Huber | [[Category: Bourenkov GP]] | ||
[[Category: Wahl | [[Category: Huber R]] | ||
[[Category: Worbs | [[Category: Wahl MC]] | ||
[[Category: Worbs M]] | |||
Latest revision as of 11:56, 9 May 2024
Crystal structure of NusA from Thermotoga maritimaCrystal structure of NusA from Thermotoga maritima
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of Thermotoga maritima NusA, a transcription factor involved in pausing, termination, and antitermination processes, reveals a four-domain, rod-shaped molecule. An N-terminal alpha/beta portion, a five-stranded beta-barrel (S1 domain), and two K-homology (KH) modules create a continuous spine of positive electrostatic potential, suitable for nonspecific mRNA attraction. Homology models suggest how, in addition, specific mRNA regulatory sequences can be recognized by the S1 and KH motifs. An arrangement of multiple S1 and KH domains mediated by highly conserved residues is seen, creating an extended RNA binding surface, a paradigm for other proteins with similar domain arrays. Structural and mutational analyses indicate that the motifs cooperate, modulating strength and specificity of RNA binding. An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA.,Worbs M, Bourenkov GP, Bartunik HD, Huber R, Wahl MC Mol Cell. 2001 Jun;7(6):1177-89. PMID:11430821[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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