3vh0: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of E. coli YncE complexed with DNA== | |||
<StructureSection load='3vh0' size='340' side='right' caption='[[3vh0]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vh0]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VH0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VH0 FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yncE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</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=3vh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vh0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vh0 RCSB], [http://www.ebi.ac.uk/pdbsum/3vh0 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
beta-Propellers are widely utilized in nature as recognition modules. The well conserved beta-propeller fold exhibits a high degree of functional diversity, which is probably accomplished through variations in the surface properties of the proteins. Little is known about the interactions between beta-propeller proteins and nucleic acids. In the present study, it has been found that the bacterial beta-propeller protein YncE binds to DNA. Crystal structures of YncE in the free form and complexed with DNA revealed that the surface region of YncE corresponding to the `canonical' substrate-binding site forms essential contacts with DNA. A single DNA base within a single-stranded DNA region is trapped in the hydrophobic pocket located within the central channel of the beta-propeller protein. These data provide physical evidence for the DNA-binding ability of the previously uncharacterized YncE and also suggest that the `canonical' substrate-binding site may be commonly adapted to facilitate nucleic acid binding in a subset of beta-propeller proteins. | |||
Structural basis for the DNA-binding activity of the bacterial beta-propeller protein YncE.,Kagawa W, Sagawa T, Niki H, Kurumizaka H Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1045-53. Epub 2011, Nov 5. PMID:22120742<ref>PMID:22120742</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
[[Category: Kagawa, W | [[Category: Kagawa, W]] | ||
[[Category: Kurumizaka, H | [[Category: Kurumizaka, H]] | ||
[[Category: Niki, H | [[Category: Niki, H]] | ||
[[Category: Sagawa, T | [[Category: Sagawa, T]] | ||
[[Category: Beta-propeller]] | [[Category: Beta-propeller]] | ||
[[Category: Protein binding-dna complex]] | [[Category: Protein binding-dna complex]] | ||