6njw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='6njw' size='340' side='right'caption='[[6njw]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
<StructureSection load='6njw' size='340' side='right'caption='[[6njw]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6njw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NJW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NJW FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6njw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xancb Xancb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NJW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NJW 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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene></td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XCCB100_2436 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=509169 XANCB])</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=6njw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6njw OCA], [http://pdbe.org/6njw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6njw RCSB], [http://www.ebi.ac.uk/pdbsum/6njw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6njw ProSAT]</span></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=6njw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6njw OCA], [http://pdbe.org/6njw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6njw RCSB], [http://www.ebi.ac.uk/pdbsum/6njw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6njw ProSAT]</span></td></tr>
</table>
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Overcoming lysogenization defect (OLD) proteins constitute a family of uncharacterized nucleases present in bacteria, archaea, and some viruses. These enzymes contain an N-terminal ATPase domain and a C-terminal Toprim domain common amongst replication, recombination, and repair proteins. The in vivo activities of OLD proteins remain poorly understood and no definitive structural information exists. Here we identify and define two classes of OLD proteins based on differences in gene neighborhood and amino acid sequence conservation and present the crystal structures of the catalytic C-terminal regions from the Burkholderia pseudomallei and Xanthamonas campestris p.v. campestris Class 2 OLD proteins at 2.24 A and 1.86 A resolution respectively. The structures reveal a two-domain architecture containing a Toprim domain with altered architecture and a unique helical domain. Conserved side chains contributed by both domains coordinate two bound magnesium ions in the active site of B. pseudomallei OLD in a geometry that supports a two-metal catalysis mechanism for cleavage. The spatial organization of these domains additionally suggests a novel mode of DNA binding that is distinct from other Toprim containing proteins. Together, these findings define the fundamental structural properties of the OLD family catalytic core and the underlying mechanism controlling nuclease activity.
 +
 +
Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavage.,Schiltz CJ, Lee A, Partlow EA, Hosford CJ, Chappie JS Nucleic Acids Res. 2019 Aug 10. pii: 5545734. doi: 10.1093/nar/gkz703. PMID:31400118<ref>PMID:31400118</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 6njw" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
 +
[[Category: Xancb]]
[[Category: Chappie, J S]]
[[Category: Chappie, J S]]
[[Category: Hosford, C J]]
[[Category: Hosford, C J]]

Revision as of 06:37, 21 August 2019

C-terminal region of the Xanthomonas campestris pv. campestris OLD protein phased with platinum

PDB ID 6njw

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools