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| - | [[Image:1ev7.gif|left|200px]]<br /><applet load="1ev7" size="450" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="1ev7, resolution 2.38Å" /> | |
| - | '''CRYSTAL STRUCTURE OF DNA RESTRICTION ENDONUCLEASE NAEI'''<br /> | |
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| - | ==Overview== | + | ==CRYSTAL STRUCTURE OF DNA RESTRICTION ENDONUCLEASE NAEI== |
| - | NAE:I is transformed from DNA endonuclease to DNA topoisomerase and, recombinase by a single amino acid substitution. The crystal structure of, NAE:I was solved at 2.3 A resolution and shows that NAE:I is a dimeric, molecule with two domains per monomer. Each domain contains one potential, DNA recognition motif corresponding to either endonuclease or, topoisomerase activity. The N-terminal domain core folds like the other, type II restriction endonucleases as well as lambda-exonuclease and the, DNA repair enzymes MutH and Vsr, implying a common evolutionary origin and, catalytic mechanism. The C-terminal domain contains a catabolite activator, protein (CAP) motif present in many DNA-binding proteins, including the, type IA and type II topoisomerases. Thus, the NAE:I structure implies that, DNA processing enzymes evolved from a few common ancestors. NAE:I may be, an evolutionary bridge between endonuclease and DNA processing enzymes.
| + | <StructureSection load='1ev7' size='340' side='right'caption='[[1ev7]], [[Resolution|resolution]] 2.38Å' scene=''> |
| | + | == Structural highlights == |
| | + | <table><tr><td colspan='2'>[[1ev7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lentzea_aerocolonigenes Lentzea aerocolonigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EV7 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]] 2.38Å</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=1ev7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ev7 OCA], [https://pdbe.org/1ev7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ev7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ev7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ev7 ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/T2N1_LENAE T2N1_LENAE] An E and P subtype restriction enzyme that recognizes the double-stranded unmethylated sequence 5'-GCCGGC-3' and cleaves after C-3.<ref>PMID:7892605</ref> <ref>PMID:8932368</ref> <ref>PMID:12654995</ref> |
| | | | |
| - | ==About this Structure== | + | ==See Also== |
| - | 1EV7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lechevalieria_aerocolonigenes Lechevalieria aerocolonigenes]. Active as [http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EV7 OCA].
| + | *[[Endonuclease 3D structures|Endonuclease 3D structures]] |
| - | | + | == References == |
| - | ==Reference== | + | <references/> |
| - | Crystal structure of NaeI-an evolutionary bridge between DNA endonuclease and topoisomerase., Huai Q, Colandene JD, Chen Y, Luo F, Zhao Y, Topal MD, Ke H, EMBO J. 2000 Jun 15;19(12):3110-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10856254 10856254]
| + | __TOC__ |
| - | [[Category: Lechevalieria aerocolonigenes]] | + | </StructureSection> |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Type II site-specific deoxyribonuclease]]
| + | [[Category: Lentzea aerocolonigenes]] |
| - | [[Category: Chen, Y.]] | + | [[Category: Chen Y]] |
| - | [[Category: Colandene, J.D.]] | + | [[Category: Colandene JD]] |
| - | [[Category: Huai, Q.]] | + | [[Category: Huai Q]] |
| - | [[Category: Luo, F.]] | + | [[Category: Luo F]] |
| - | [[Category: Zhao, Y.]] | + | [[Category: Zhao Y]] |
| - | [[Category: apo-naei]]
| + | |
| - | [[Category: cap]]
| + | |
| - | [[Category: helix-turn-helix]]
| + | |
| - | [[Category: restriction endonuclease]]
| + | |
| - | [[Category: topoisomerase]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:20:42 2007''
| + | |
| Structural highlights
Function
T2N1_LENAE An E and P subtype restriction enzyme that recognizes the double-stranded unmethylated sequence 5'-GCCGGC-3' and cleaves after C-3.[1] [2] [3]
See Also
References
- ↑ Jo K, Topal MD. DNA topoisomerase and recombinase activities in Nae I restriction endonuclease. Science. 1995 Mar 24;267(5205):1817-20. doi: 10.1126/science.7892605. PMID:7892605 doi:http://dx.doi.org/10.1126/science.7892605
- ↑ Jo K, Topal MD. Effects on NaeI-DNA recognition of the leucine to lysine substitution that transforms restriction endonuclease NaeI to a topoisomerase: a model for restriction endonuclease evolution. Nucleic Acids Res. 1996 Nov 1;24(21):4171-5. doi: 10.1093/nar/24.21.4171. PMID:8932368 doi:http://dx.doi.org/10.1093/nar/24.21.4171
- ↑ Roberts RJ, Belfort M, Bestor T, Bhagwat AS, Bickle TA, Bitinaite J, Blumenthal RM, Degtyarev SKh, Dryden DT, Dybvig K, Firman K, Gromova ES, Gumport RI, Halford SE, Hattman S, Heitman J, Hornby DP, Janulaitis A, Jeltsch A, Josephsen J, Kiss A, Klaenhammer TR, Kobayashi I, Kong H, Kruger DH, Lacks S, Marinus MG, Miyahara M, Morgan RD, Murray NE, Nagaraja V, Piekarowicz A, Pingoud A, Raleigh E, Rao DN, Reich N, Repin VE, Selker EU, Shaw PC, Stein DC, Stoddard BL, Szybalski W, Trautner TA, Van Etten JL, Vitor JM, Wilson GG, Xu SY. A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes. Nucleic Acids Res. 2003 Apr 1;31(7):1805-12. PMID:12654995
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