View source for 3vcf


==SSV1 integrase C-terminal catalytic domain (174-335aa)==
<StructureSection load='3vcf' size='340' side='right'caption='[[3vcf]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3vcf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_spindle-shaped_virus_1 Sulfolobus spindle-shaped virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VCF 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]] 2.7&#8491;</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=3vcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vcf OCA], [https://pdbe.org/3vcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vcf RCSB], [https://www.ebi.ac.uk/pdbsum/3vcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vcf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VINT_SSV1 VINT_SSV1] This protein may encode a site-specific integrase, which is necessary for integration of the phage by site-specific recombination into a tRNA gene of the host chromosome. Essential for virus infection.<ref>PMID:10430570</ref> <ref>PMID:22683788</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The spindle-shaped virus SSV1 of the hyperthermophilic archaeon Sulfolobus shibatae encodes an integrase (SSV1 Int). Here, the crystal structure of the C-terminal catalytic domain of SSV1 Int is reported. This is the first structural study of an archaeal tyrosine recombinase. Structural comparison shows that the C-terminal domain of SSV1 Int possesses a core fold similar to those of tyrosine recombinases of both bacterial and eukaryal origin, apart from the lack of a conserved helix corresponding to alphaI of Cre, indicating conservation of these enzymes among all three domains of life. Five of the six catalytic residues cluster around a basic cleft on the surface of the structure and the nucleophile Tyr314 is located on a flexible loop that stretches away from the central cleft, supporting the possibility that SSV1 Int cleaves the target DNA in a trans mode. Biochemical analysis suggests that the N-terminal domain is responsible for the dimerization of SSV1 Int. The C-terminal domain is capable of DNA cleavage and ligation, but at efficiencies significantly lower than those of the full-length protein. In addition, neither the N-terminal domain alone nor the C-terminal domain alone shows a strong sequence preference in DNA binding. Therefore, recognition of the core-type sequence and efficient catalysis by SSV1 Int presumably requires covalent linkage and interdomain communication between the two domains.

Structural and functional characterization of the C-terminal catalytic domain of SSV1 integrase.,Zhan Z, Ouyang S, Liang W, Zhang Z, Liu ZJ, Huang L Acta Crystallogr D Biol Crystallogr. 2012 Jun;68(Pt 6):659-70. doi:, 10.1107/S0907444912007202. Epub 2012 May 17. PMID:22683788<ref>PMID:22683788</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vcf" style="background-color:#fffaf0;"></div>

==See Also==
*[[Retroviral integrase 3D structures|Retroviral integrase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sulfolobus spindle-shaped virus 1]]
[[Category: Huang L]]
[[Category: Liang W]]
[[Category: Liu Z-J]]
[[Category: Ouyang S]]