1sd5

<StructureSection load='1sd5' size='340' side='right' caption='[[1sd5]], [[Resolution|resolution]] 1.68&Aring;' scene=''>

<table><tr><td colspan='2'>[[1sd5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SD5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SD5 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1s8n|1s8n]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rv1626 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=1sd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sd5 OCA], [http://pdbe.org/1sd5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sd5 RCSB], [http://www.ebi.ac.uk/pdbsum/1sd5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sd5 ProSAT], [http://www.topsan.org/Proteins/XMTB/1sd5 TOPSAN]</span></td></tr>

[[http://www.uniprot.org/uniprot/PDTAR_MYCTU PDTAR_MYCTU]] Member of the two-component regulatory system pdtaR/pdtaS.<ref>PMID:16026786</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

We describe the crystal structure of Rv1626 from Mycobacterium tuberculosis at 1.48 A resolution and the corresponding solution structure determined from small angle X-ray scattering. The N-terminal domain shows structural homology to the receiver domains found in bacterial two-component systems. The C-terminal domain has high structural homology to a recently discovered RNA binding domain involved in transcriptional antitermination. The molecule in solution was found to be monomeric as it is in the crystal, but in solution it undergoes a conformational change that is triggered by changes in ionic strength. This is the first structure that links the phosphorylation cascade of the two-component systems with the antitermination event in the transcriptional machinery. Rv1626 belongs to a family of proteins, which we propose calling phosphorylation-dependent transcriptional antitermination regulators, so far only found in bacteria, and includes NasT, a protein from the assimilatory nitrate/nitrite reductase operon of Azetobacter vinelandii.

The crystal and solution structure of a putative transcriptional antiterminator from Mycobacterium tuberculosis.,Morth JP, Feng V, Perry LJ, Svergun DI, Tucker PA Structure. 2004 Sep;12(9):1595-605. PMID:15341725<ref>PMID:15341725</ref>

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

</div>

<div class="pdbe-citations 1sd5" style="background-color:#fffaf0;"></div>

[[Category: Myctu]]

[[Category: Feng, V]]

[[Category: Morth, J P]]

[[Category: Perry, L J]]

[[Category: Svergun, D I]]

[[Category: Structural genomic]]

[[Category: Tucker, P A]]

[[Category: Unknown function]]