4wuz: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "4wuz" [edit=sysop:move=sysop] |
No edit summary |
||
| (7 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of lambda exonuclease in complex with DNA and Ca2+== | ==Crystal structure of lambda exonuclease in complex with DNA and Ca2+== | ||
<StructureSection load='4wuz' size='340' side='right' caption='[[4wuz]], [[Resolution|resolution]] 2.38Å' scene=''> | <StructureSection load='4wuz' size='340' side='right'caption='[[4wuz]], [[Resolution|resolution]] 2.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wuz]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WUZ OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4wuz]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda] 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=4WUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WUZ FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wuz OCA], [https://pdbe.org/4wuz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wuz RCSB], [https://www.ebi.ac.uk/pdbsum/4wuz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wuz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/EXO_LAMBD EXO_LAMBD] Facilitates phage DNA recombination through the double-strand break repair (DSBR) and single-strand annealing pathways. Also important for the late, rolling-circle mode of lambda DNA replication. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacteriophage lambda exonuclease (lambdaexo) is a ring-shaped homotrimer that resects double-stranded DNA ends in the 5'-3' direction to generate a long 3'-overhang that is a substrate for recombination. lambdaexo is a member of the type II restriction endonuclease-like superfamily of proteins that use a Mg2+-dependent mechanism for nucleotide cleavage. A previous structure of lambdaexo in complex with DNA and Mg2+ was determined using a nuclease defective K131A variant to trap a stable complex. This structure revealed the detailed coordination of the two active site Mg2+ ions but did not show the interactions involving the side chain of the conserved active site Lys-131 residue. Here, we have determined the crystal structure of wild-type (WT) lambdaexo in complex with the same DNA substrate, but in the presence of Ca2+ instead of Mg2+. Surprisingly, there is only one Ca2+ bound in the active site, near the position of MgA in the structure with Mg2+. The scissile phosphate is displaced by 2.2 A relative to its position in the structure with Mg2+, and the network of interactions involving the attacking water molecule is broken. Thus, the structure does not represent a catalytic configuration. However, the crystal structure does show clear electron density for the side chain of Lys-131, which is held in place by interactions with Gln-157 and Glu-129. By combining the K131A-Mg2+ and WT-Ca2+ structures, we constructed a composite model to show the likely interactions of Lys-131 during catalysis. The implications with regard to the catalytic mechanism are discussed. | |||
Crystal Structure of lambda Exonuclease in Complex with DNA and Ca,Zhang J, Pan X, Bell CE Biochemistry. 2014 Nov 19. PMID:25370446<ref>PMID:25370446</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4wuz" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Exonuclease 3D structures|Exonuclease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia virus Lambda]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Bell CE]] | ||
[[Category: Zhang J]] | |||