5c32: Difference between revisions
New page: '''Unreleased structure''' The entry 5c32 is ON HOLD Authors: Trejo, C.S., Rice, P.A. Description: Category: Unreleased Structures Category: Trejo, C.S Category: Rice, P.A |
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==Constitutively active Sin recombinase cataltyic domain - I100T== | |||
<StructureSection load='5c32' size='340' side='right'caption='[[5c32]], [[Resolution|resolution]] 3.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5c32]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C32 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]] 3.053Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5c32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c32 OCA], [https://pdbe.org/5c32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c32 RCSB], [https://www.ebi.ac.uk/pdbsum/5c32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c32 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BIN3_STAAU BIN3_STAAU] Potential DNA invertase. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Members of the serine family of site-specific recombinases exchange DNA strands via 180 degrees rotation about a central protein-protein interface. Modeling of this process has been hampered by the lack of structures in more than one rotational state for any individual serine recombinase. Here we report crystal structures of the catalytic domains of four constitutively active mutants of the serine recombinase Sin, providing snapshots of rotational states not previously visualized for Sin, including two seen in the same crystal. Normal mode analysis predicted that each tetramer's lowest frequency mode (i.e. most accessible large-scale motion) mimics rotation: two protomers rotate as a pair with respect to the other two. Our analyses also suggest that rotation is not a rigid body movement around a single symmetry axis but instead uses multiple pivot points and entails internal motions within each subunit. | |||
Snapshots of a molecular swivel in action.,Trejo CS, Rock RS, Stark WM, Boocock MR, Rice PA Nucleic Acids Res. 2018 Jun 1;46(10):5286-5296. doi: 10.1093/nar/gkx1309. PMID:29315406<ref>PMID:29315406</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5c32" style="background-color:#fffaf0;"></div> | ||
[[Category: Rice | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus]] | |||
[[Category: Rice PA]] | |||
[[Category: Trejo CS]] | |||
Latest revision as of 06:55, 21 November 2024
Constitutively active Sin recombinase cataltyic domain - I100TConstitutively active Sin recombinase cataltyic domain - I100T
Structural highlights
FunctionBIN3_STAAU Potential DNA invertase. Publication Abstract from PubMedMembers of the serine family of site-specific recombinases exchange DNA strands via 180 degrees rotation about a central protein-protein interface. Modeling of this process has been hampered by the lack of structures in more than one rotational state for any individual serine recombinase. Here we report crystal structures of the catalytic domains of four constitutively active mutants of the serine recombinase Sin, providing snapshots of rotational states not previously visualized for Sin, including two seen in the same crystal. Normal mode analysis predicted that each tetramer's lowest frequency mode (i.e. most accessible large-scale motion) mimics rotation: two protomers rotate as a pair with respect to the other two. Our analyses also suggest that rotation is not a rigid body movement around a single symmetry axis but instead uses multiple pivot points and entails internal motions within each subunit. Snapshots of a molecular swivel in action.,Trejo CS, Rock RS, Stark WM, Boocock MR, Rice PA Nucleic Acids Res. 2018 Jun 1;46(10):5286-5296. doi: 10.1093/nar/gkx1309. PMID:29315406[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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