2cmp: Difference between revisions
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<StructureSection load='2cmp' size='340' side='right'caption='[[2cmp]], [[Resolution|resolution]] 1.58Å' scene=''> | <StructureSection load='2cmp' size='340' side='right'caption='[[2cmp]], [[Resolution|resolution]] 1.58Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2cmp]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2cmp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_phage_SF6 Bacillus phage SF6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CMP FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58Å</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=2cmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cmp OCA], [https://pdbe.org/2cmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cmp RCSB], [https://www.ebi.ac.uk/pdbsum/2cmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cmp ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TERS_BPSF6 TERS_BPSF6] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Terminase|Terminase]] | *[[Terminase 3D Structures|Terminase 3D Structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus phage SF6]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Alonso | [[Category: Alonso JC]] | ||
[[Category: Antson | [[Category: Antson AA]] | ||
[[Category: Benini | [[Category: Benini S]] | ||
[[Category: Chechik | [[Category: Chechik M]] | ||
[[Category: DeLuchi | [[Category: DeLuchi D]] | ||
[[Category: Ortiz-Lombardia | [[Category: Ortiz-Lombardia M]] | ||
[[Category: Polier | [[Category: Polier S]] | ||
[[Category: Shevtsov | [[Category: Shevtsov MB]] | ||
Latest revision as of 12:28, 9 May 2024
crystal structure of the DNA binding domain of G1P SMALL TERMINASE SUBUNIT from bacteriophage SF6crystal structure of the DNA binding domain of G1P SMALL TERMINASE SUBUNIT from bacteriophage SF6
Structural highlights
FunctionEvolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDNA packaging in tailed bacteriophages and in evolutionarily related herpesviruses is controlled by a viral-encoded terminase. As in a number of other phages, in the Bacillus subtilis bacteriophages SF6 and SPP1 the terminase complex consists of two proteins: G1P and G2P. The crystal structure of the N-terminal DNA-binding domain of the bacteriophage SF6 small terminase subunit G1P is reported. Structural comparison with other DNA-binding proteins allows a general model for the interaction of G1P with the packaging-initiation site to be proposed. The 1.58 A resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding.,Benini S, Chechik M, Ortiz Lombardia M, Polier S, Leech A, Shevtsov MB, Alonso JC Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Apr 1;69(Pt 4):376-81., doi: 10.1107/S1744309113004399. Epub 2013 Mar 28. PMID:23545641[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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