2wkc: Difference between revisions
New page: '''Unreleased structure''' The entry 2wkc is ON HOLD until Paper Publication Authors: Scaltriti, E., Cambillau, C., Ortiz-Lombardia, M. Description: Crystal structure from a single-str... |
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==Crystal structure from a single-stranded DNA binding protein from the lactococcal phage p2== | |||
<StructureSection load='2wkc' size='340' side='right'caption='[[2wkc]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2wkc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_virus_P2 Lactococcus virus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WKC 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]] 2.6Å</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=2wkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wkc OCA], [https://pdbe.org/2wkc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wkc RCSB], [https://www.ebi.ac.uk/pdbsum/2wkc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wkc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q09WL7_9CAUD Q09WL7_9CAUD] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wk/2wkc_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2wkc ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lactococcus lactis, a Gram-positive bacterium widely used by the dairy industry, is subject to infection by a diverse population of virulent phages, predominantly by those of the 936 group, including the siphovirus phage p2. Confronted with the negative impact of phage infection on milk fermentation, the study of the biology of lactococcal provides insight from applied and fundamental perspectives. We decided to characterize the product of the orf34 gene from lactococcus phage p2, which was considered as a candidate single-stranded DNA binding protein (SSB) due to its localization downstream of a gene coding for a single-strand annealing protein. Two-dimensional gel electrophoresis showed that ORF34(p2) is expressed in large amounts during the early phases of phage infection, suggesting an important role in this process. Gel-shift assays, surface plasmon resonance and atomic force microscopy demonstrated that ORF34(p2) interacts with single-strand DNA with nanomolar affinity. We also determined the crystal structure of ORF34(p2) and showed that it bears a variation of the typical oligonucleotide/oligosaccharide binding-fold of SSBs. Finally, we found that ORF34(p2) is able to stimulate Escherichia coli RecA-mediated homologous recombination. The specific structural and biochemical properties that distinguish ORF34(p2) from other SSB proteins are discussed. | |||
Structure and function of phage p2 ORF34(p2), a new type of single-stranded DNA binding protein.,Scaltriti E, Tegoni M, Rivetti C, Launay H, Masson JY, Magadan AH, Tremblay D, Moineau S, Ramoni R, Lichiere J, Campanacci V, Cambillau C, Ortiz-Lombardia M Mol Microbiol. 2009 Sep;73(6):1156-70. Epub 2009 Aug 25. PMID:19719513<ref>PMID:19719513</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2wkc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lactococcus virus P2]] | |||
[[Category: Large Structures]] | |||
[[Category: Cambillau C]] | |||
[[Category: Ortiz-Lombardia M]] | |||
[[Category: Scaltriti E]] | |||
Latest revision as of 18:59, 13 December 2023
Crystal structure from a single-stranded DNA binding protein from the lactococcal phage p2Crystal structure from a single-stranded DNA binding protein from the lactococcal phage p2
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 PubMedLactococcus lactis, a Gram-positive bacterium widely used by the dairy industry, is subject to infection by a diverse population of virulent phages, predominantly by those of the 936 group, including the siphovirus phage p2. Confronted with the negative impact of phage infection on milk fermentation, the study of the biology of lactococcal provides insight from applied and fundamental perspectives. We decided to characterize the product of the orf34 gene from lactococcus phage p2, which was considered as a candidate single-stranded DNA binding protein (SSB) due to its localization downstream of a gene coding for a single-strand annealing protein. Two-dimensional gel electrophoresis showed that ORF34(p2) is expressed in large amounts during the early phases of phage infection, suggesting an important role in this process. Gel-shift assays, surface plasmon resonance and atomic force microscopy demonstrated that ORF34(p2) interacts with single-strand DNA with nanomolar affinity. We also determined the crystal structure of ORF34(p2) and showed that it bears a variation of the typical oligonucleotide/oligosaccharide binding-fold of SSBs. Finally, we found that ORF34(p2) is able to stimulate Escherichia coli RecA-mediated homologous recombination. The specific structural and biochemical properties that distinguish ORF34(p2) from other SSB proteins are discussed. Structure and function of phage p2 ORF34(p2), a new type of single-stranded DNA binding protein.,Scaltriti E, Tegoni M, Rivetti C, Launay H, Masson JY, Magadan AH, Tremblay D, Moineau S, Ramoni R, Lichiere J, Campanacci V, Cambillau C, Ortiz-Lombardia M Mol Microbiol. 2009 Sep;73(6):1156-70. Epub 2009 Aug 25. PMID:19719513[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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