| 词条 | R.EcoRII | ||
| 释义 |
Mode of actionEcoRII is a bacterial Type IIE[2] REase that interacts with two[3] or three[4] copies of the pseudopalindromic DNA recognition sequence 5'-CCWGG-3' (W = A or T), one being the actual target of cleavage, the other(s) serving as the allosteric activator(s). EcoRII cut target DNA sequence CCWGG generating sticky ends.[5] Cut diagram
Structure{{Infobox protein family| Symbol = EcoRII-N | Name = Restriction endonuclease EcoRII, N-terminal | image = PDB 1na6 EBI.jpg | width = | caption = crystal structure of restriction endonuclease ecorii mutant r88a | Pfam = PF09217 | Pfam_clan = CL0405 | InterPro = IPR015300 | SMART = | PROSITE = | MEROPS = | SCOP = 1na6 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }}{{Infobox protein family | Symbol = EcoRII-C | Name = EcoRII C terminal | image = PDB 1na6 EBI.jpg | width = | caption = crystal structure of restriction endonuclease ecorii mutant r88a | Pfam = PF09019 | Pfam_clan = CL0236 | InterPro = IPR015109 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} The apo crystal structure of EcoRII mutant R88A ({{PDB|1NA6}})[6] has been solved at 2.1 Å resolution. The EcoRII monomer has two domains, N-terminal and C-terminal, linked through a hinge loop. Effector-binding domainThe N-terminal effector-binding domain has an archetypal DNA-binding pseudobarrel fold ({{SCOP|101936}}) with a prominent cleft. Structural superposition showed it is evolutionarily related to:
Catalytic domainThe C-terminal catalytic domain has a typical[10] restriction endonuclease-like fold ({{SCOP|52979}}) and belongs to the large (more than 30 members) restriction endonuclease superfamily ({{SCOP|52980}}). Autoinhibition/activation mechanismStructure-based sequence alignment and site-directed mutagenesis identified the putative PD..D/EXK active sites of the EcoRII catalytic domain dimer that in apo structure are spatially blocked by the N-terminal domains.[6]See also
External links
References1. ^{{cite web | url = http://rebase.neb.com/rebase/enz/EcoRII.html | title = EcoRII | accessdate = 2008-03-23 | author = Richard J. Roberts | date = | work = REBASE - The Restriction Enzyme Database | publisher = | pages = | language = | archiveurl = | archivedate = | quote = }} {{Esterases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{Nucleases}}{{DEFAULTSORT:R.Ecorii}}2. ^{{cite journal |vauthors=Roberts RJ, Belfort M, Bestor T, etal | title = A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes | journal = Nucleic Acids Res. | volume = 31 | issue = 7 | pages = 1805–12 | year = 2003 | pmid = 12654995 | doi = 10.1093/nar/gkg274 | pmc = 152790 }} PDF 3. ^{{cite journal |vauthors=Mücke M, Lurz R, Mackeldanz P, Behlke J, Krüger DH, Reuter M | title = Imaging DNA loops induced by restriction endonuclease EcoRII. A single amino acid substitution uncouples target recognition from cooperative DNA interaction and cleavage | journal = J. Biol. Chem. | volume = 275 | issue = 39 | pages = 30631–7 | year = 2000 | pmid = 10903314 | doi = 10.1074/jbc.M003904200 }}PDF 4. ^{{cite journal |vauthors=Shlyakhtenko LS, Gilmore J, Portillo A, Tamulaitis G, Siksnys V, Lyubchenko YL | title = Direct visualization of the EcoRII-DNA triple synaptic complex by atomic force microscopy | journal = Biochemistry | volume = 46 | issue = 39 | pages = 11128–36 | year = 2007 | pmid = 17845057 | doi = 10.1021/bi701123u }} 5. ^{{cite book | author = Griffiths, Anthony J. F. | title = An Introduction to genetic analysis | publisher = W.H. Freeman | location = San Francisco | year = 1999 | pages = | isbn = 978-0-7167-3520-5 | oclc = | doi = }} 6. ^1 {{cite journal |vauthors=Zhou XE, Wang Y, Reuter M, Mücke M, Krüger DH, Meehan EJ, Chen L | title = Crystal structure of type IIE restriction endonuclease EcoRII reveals an autoinhibition mechanism by a novel effector-binding fold | journal = J. Mol. Biol. | volume = 335 | issue = 1 | pages = 307–19 | year = 2004 | pmid = 14659759 | doi = 10.1016/j.jmb.2003.10.030 }} 7. ^{{cite journal |vauthors=Yamasaki K, Kigawa T, Inoue M, Tateno M, Yamasaki T, Yabuki T, Aoki M, Seki E, Matsuda T, Tomo Y, Hayami N, Terada T, Shirouzu M, Osanai T, Tanaka A, Seki M, Shinozaki K, Yokoyama S | title = Solution structure of the B3 DNA binding domain of the Arabidopsis cold-responsive transcription factor RAV1 | journal = Plant Cell | volume = 16 | issue = 12 | pages = 3448–59 | year = 2004 | pmid = 15548737 | doi = 10.1105/tpc.104.026112 | pmc = 535885 }}PDF 8. ^{{cite web | url = http://rebase.neb.com/rebase/enz/BfiI.html | title = BfiI | accessdate = 2008-03-23 | author = Richard J. Roberts | date = | work = REBASE - The Restriction Enzyme Database | publisher = | pages = | language = | archiveurl = | archivedate = | quote = }} 9. ^{{cite journal |vauthors=Grazulis S, Manakova E, Roessle M, Bochtler M, Tamulaitiene G, Huber R, Siksnys V | title = Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nuclease | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 102 | issue = 44 | pages = 15797–802 | year = 2005 | pmid = 16247004 | doi = 10.1073/pnas.0507949102 | pmc = 1266039 | url = http://bib-pubdb1.desy.de/record/138680/files/2005_Grazulis_15797.pdf }} PDF 10. ^{{cite journal |vauthors=Niv MY, Ripoll DR, Vila JA, Liwo A, Vanamee ES, Aggarwal AK, Weinstein H, Scheraga HA | title = Topology of Type II REases revisited; structural classes and the common conserved core | journal = Nucleic Acids Research | volume = 35 | issue = 7 | pages = 2227–37 | year = 2007 | pmid = 17369272 | doi = 10.1093/nar/gkm045 | pmc = 1874628}} 6 : EC 3.1.21|Molecular biology|Bacterial enzymes|Restriction enzymes|EC 3.1|Nucleases |
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