1p7d
From Proteopedia
(Difference between revisions)
Line 3: | Line 3: | ||
<StructureSection load='1p7d' size='340' side='right'caption='[[1p7d]], [[Resolution|resolution]] 2.95Å' scene=''> | <StructureSection load='1p7d' size='340' side='right'caption='[[1p7d]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1p7d]] is a 6 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1p7d]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P7D 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]] 2.95Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</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=1p7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p7d OCA], [https://pdbe.org/1p7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p7d RCSB], [https://www.ebi.ac.uk/pdbsum/1p7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p7d ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/VINT_LAMBD VINT_LAMBD] Integrase is necessary for integration of the phage into the host genome by site-specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 20: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1p7d ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1p7d ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The bacteriophage lambda integrase protein (lambda Int) belongs to a family of tyrosine recombinases that catalyze DNA rearrangements. We have determined a crystal structure of lambda Int complexed with a cleaved DNA substrate through a covalent phosphotyrosine bond. In comparison to an earlier unliganded structure, we observe a drastic conformational change in DNA-bound lambda Int that brings Tyr342 into the active site for cleavage of the DNA in cis. A flexible linker connects the central and the catalytic domains, allowing the protein to encircle the DNA. Binding specificity is achieved through direct interactions with the DNA and indirect readout of the flexibility of the att site. The conformational switch that activates lambda Int for DNA cleavage exposes the C-terminal 8 residues for interactions with a neighboring Int molecule. The protein interactions mediated by lambda Int's C-terminal tail offer a mechanism for the allosteric control of cleavage activity in higher order lambda Int complexes. | ||
- | |||
- | A conformational switch controls the DNA cleavage activity of lambda integrase.,Aihara H, Kwon HJ, Nunes-Duby SE, Landy A, Ellenberger T Mol Cell. 2003 Jul;12(1):187-98. PMID:12887904<ref>PMID:12887904</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1p7d" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Retroviral integrase 3D structures|Retroviral integrase 3D structures]] | *[[Retroviral integrase 3D structures|Retroviral integrase 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Escherichia virus Lambda]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Aihara | + | [[Category: Aihara H]] |
- | [[Category: Ellenberger | + | [[Category: Ellenberger T]] |
- | [[Category: Kwon | + | [[Category: Kwon HJ]] |
- | [[Category: Landy | + | [[Category: Landy A]] |
- | [[Category: Nunes-Duby | + | [[Category: Nunes-Duby SE]] |
- | + | ||
- | + |
Revision as of 05:53, 17 April 2024
Crystal structure of the Lambda Integrase (residues 75-356) bound to DNA
|