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1aih
From Proteopedia
(Difference between revisions)
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<StructureSection load='1aih' size='340' side='right'caption='[[1aih]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1aih' size='340' side='right'caption='[[1aih]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1aih]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1aih]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_virus_HP1 Haemophilus virus HP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AIH 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]] 2.5Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aih OCA], [https://pdbe.org/1aih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aih RCSB], [https://www.ebi.ac.uk/pdbsum/1aih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aih ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/VINT_BPHC1 VINT_BPHC1] 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]] | ||
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</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=1aih 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=1aih ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | HP1 integrase promotes site-specific recombination of the HP1 genome into that of Haemophilus influenzae. The isolated C-terminal domain (residues 165-337) of the protein interacts with the recombination site and contains the four catalytic residues conserved in the integrase family. This domain represents a novel fold consisting principally of well-packed alpha helices, a surface beta sheet, and an ordered 17-residue C-terminal tail. The conserved triad of basic residues and the active-site tyrosine are contributed by a single monomer and occupy fixed positions in a defined active-site cleft. Dimers are formed by mutual interactions of the tail of one monomer with an adjacent monomer; this orients active-site clefts antiparallel to each other. | ||
| - | |||
| - | Molecular organization in site-specific recombination: the catalytic domain of bacteriophage HP1 integrase at 2.7 A resolution.,Hickman AB, Waninger S, Scocca JJ, Dyda F Cell. 1997 Apr 18;89(2):227-37. PMID:9108478<ref>PMID:9108478</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1aih" 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: Haemophilus virus HP1]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Dyda | + | [[Category: Dyda F]] |
| - | [[Category: Hickman | + | [[Category: Hickman AB]] |
| - | [[Category: Scocca | + | [[Category: Scocca JJ]] |
| - | [[Category: Waninger | + | [[Category: Waninger S]] |
| - | + | ||
| - | + | ||
Current revision
CATALYTIC DOMAIN OF BACTERIOPHAGE HP1 INTEGRASE
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