View source for 6jrg


==Crystal structure of ZmMoc1 H253A mutant in complex with Holliday junction==
<StructureSection load='6jrg' size='340' side='right'caption='[[6jrg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jrg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JRG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JRG 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]] 2.005&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6jrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jrg OCA], [https://pdbe.org/6jrg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jrg RCSB], [https://www.ebi.ac.uk/pdbsum/6jrg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jrg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B4FCI7_MAIZE B4FCI7_MAIZE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Holliday junction (HJ) is a key intermediate during homologous recombination and DNA double-strand break repair. Timely HJ resolution by resolvases is critical for maintaining genome stability. The mechanisms underlying sequence-specific substrate recognition and cleavage by resolvases remain elusive. The monokaryotic chloroplast 1 protein (MOC1) specifically cleaves four-way DNA junctions in a sequence-specific manner. Here, we report the crystal structures of MOC1 from Zea mays, alone or bound to HJ DNA. MOC1 uses a unique beta-hairpin to embrace the DNA junction. A base-recognition motif specifically interacts with the junction center, inducing base flipping and pseudobase-pair formation at the strand-exchanging points. Structures of MOC1 bound to HJ and different metal ions support a two-metal ion catalysis mechanism. Further molecular dynamics simulations and biochemical analyses reveal a communication between specific substrate recognition and metal ion-dependent catalysis. Our study thus provides a mechanism for how a resolvase turns substrate specificity into catalytic efficiency.

Structural basis of sequence-specific Holliday junction cleavage by MOC1.,Lin H, Zhang D, Zuo K, Yuan C, Li J, Huang M, Lin Z Nat Chem Biol. 2019 Oct 14. pii: 10.1038/s41589-019-0377-4. doi:, 10.1038/s41589-019-0377-4. PMID:31611704<ref>PMID:31611704</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jrg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Zea mays]]
[[Category: Lin H]]
[[Category: Lin Z]]
[[Category: Yuan C]]
[[Category: Zhang D]]