View source for 4mv2


==Crystal structure of plu4264 protein from Photorhabdus luminescens==
<StructureSection load='4mv2' size='340' side='right' caption='[[4mv2]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4mv2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pholl Pholl]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4i4a 4i4a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MV2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MV2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">plu4264 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243265 PHOLL])</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=4mv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mv2 OCA], [http://pdbe.org/4mv2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mv2 RCSB], [http://www.ebi.ac.uk/pdbsum/4mv2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mv2 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Proteins belonging to the cupin superfamily have a wide range of catalytic and non-catalytic functions. Cupin proteins commonly have the capacity to bind a metal ion with the metal frequently determining the function of the protein. We have been investigating the function of homologous cupin proteins that are conserved in more than 40 species of bacteria. To gain insights into the potential function of these proteins we have solved the structure of Plu4264 from Photorhabdus luminescens TTO1 at a resolution of 1.35 A and identified manganese as the likely natural metal ligand of the protein. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.

Structure of a cupin protein Plu4264 from Photorhabdus luminescens subsp. laumondii TTO1 at 1.35 A resolution.,Weerth RS, Michalska K, Bingman CA, Yennamalli RM, Li H, Jedrzejczak R, Wang F, Babnigg G, Joachimiak A, Thomas MG, Phillips GN Proteins. 2014 Oct 30. doi: 10.1002/prot.24705. PMID:25354690<ref>PMID:25354690</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4mv2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Pholl]]
[[Category: Babnigg, G]]
[[Category: Bingman, C A]]
[[Category: Jedrzejczak, R]]
[[Category: Joachimiak, A]]
[[Category: Li, H]]
[[Category: Structural genomic]]
[[Category: Michalska, K]]
[[Category: NatPro, Enzyme Discovery for Natural Product Biosynthesis]]
[[Category: Phillips, G N]]
[[Category: Thomas, M G]]
[[Category: Weerth, S]]
[[Category: Yennamalli, R]]
[[Category: Cupin]]
[[Category: Enzyme discovery for natural product biosynthesis]]
[[Category: Mcsg]]
[[Category: Natpro]]
[[Category: Psi-biology]]
[[Category: Unknown function]]