View source for 8efz


==Crystal structure of CcNikZ-II, apoprotein==
<StructureSection load='8efz' size='340' side='right'caption='[[8efz]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8efz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_carboxidivorans_P7 Clostridium carboxidivorans P7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EFZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8efz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8efz OCA], [https://pdbe.org/8efz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8efz RCSB], [https://www.ebi.ac.uk/pdbsum/8efz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8efz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C6PRH6_9CLOT C6PRH6_9CLOT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Extracytoplasmic Ni(II)-binding proteins (NiBPs) are molecular shuttles involved in cellular nickel uptake. Here, we determined the crystal structure of apo CcNikZ-II at 2.38 A, which revealed a Ni(II)-binding site comprised of the double His (HH-)prong (His511, His512) and a short variable (v-)loop nearby (Thr59-Thr64, TEDKYT). Mutagenesis of the site identified Glu60 and His511 as critical for high affinity Ni(II)-binding. Phylogenetic analysis showed 15 protein clusters with two groups containing the HH-prong. Metal-binding assays with 11 purified NiBPs containing this feature yielded higher Ni(II)-binding affinities. Replacement of the wild type v-loop with those from other NiBPs improved the affinity by up to an order of magnitude. This work provides molecular insights into the determinants for Ni(II) affinity and paves way for NiBP engineering.

Ni(II)-binding affinity of CcNikZ-II and its homologs: the role of the HH-prong and variable loop revealed by structural and mutational studies.,Diep P, Stogios PJ, Evdokimova E, Savchenko A, Mahadevan R, Yakunin AF FEBS J. 2024 Jul;291(13):2980-2993. doi: 10.1111/febs.17125. Epub 2024 Mar 31. PMID:38555564<ref>PMID:38555564</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8efz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium carboxidivorans P7]]
[[Category: Large Structures]]
[[Category: Diep P]]
[[Category: Evdokimova E]]
[[Category: Mahadevan K]]
[[Category: Savchenko A]]
[[Category: Stogios PJ]]
[[Category: Yakunin A]]