3qhs: Difference between revisions
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==Crystal structure of full-length Hfq from Escherichia coli== | |||
=== | <StructureSection load='3qhs' size='340' side='right' caption='[[3qhs]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3qhs]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QHS FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qo3|3qo3]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4172, hfq, JW4130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3qhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qhs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qhs RCSB], [http://www.ebi.ac.uk/pdbsum/3qhs PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structure of full-length host factor Qbeta (Hfq) from Escherichia coli obtained from a crystal belonging to space group P1, with unit-cell parameters a = 61.91, b = 62.15, c = 81.26 A, alpha = 78.6, beta = 86.2, gamma = 59.9 degrees , was solved by molecular replacement to a resolution of 2.85 A and refined to R(work) and R(free) values of 20.7% and 25.0%, respectively. Hfq from E. coli has previously been crystallized and the structure has been solved for the N-terminal 72 amino acids, which cover approximately 65% of the full-length sequence. Here, the purification, crystallization and structural data of the full 102-amino-acid protein are presented. These data revealed that the presence of the C-terminus changes the crystal packing of E. coli Hfq. The crystal structure is discussed in the context of the recently published solution structure of Hfq from E. coli. | |||
Structural analysis of full-length Hfq from Escherichia coli.,Beich-Frandsen M, Vecerek B, Sjoblom B, Blasi U, Djinovic-Carugo K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt, 5):536-40. Epub 2011 Apr 20. PMID:21543856<ref>PMID:21543856</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Beich-Frandsen, M | [[Category: Beich-Frandsen, M]] | ||
[[Category: Blaesi, U | [[Category: Blaesi, U]] | ||
[[Category: Djinovic-Carugo, K | [[Category: Djinovic-Carugo, K]] | ||
[[Category: Sjoeblom, B | [[Category: Sjoeblom, B]] | ||
[[Category: Vecerek, B | [[Category: Vecerek, B]] | ||
[[Category: Pleiotropic regulator]] | [[Category: Pleiotropic regulator]] | ||
[[Category: Rna binding protein]] | [[Category: Rna binding protein]] | ||
[[Category: Sm-like]] | [[Category: Sm-like]] |