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| | <StructureSection load='1b7e' size='340' side='right'caption='[[1b7e]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='1b7e' size='340' side='right'caption='[[1b7e]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1b7e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B7E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1b7e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B7E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPT:2,2 6,2-TERPYRIDINE+PLATINUM(II)+CHLORIDE'>TPT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b7e OCA], [http://pdbe.org/1b7e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b7e RCSB], [http://www.ebi.ac.uk/pdbsum/1b7e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1b7e ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TPT:2,2 6,2-TERPYRIDINE+PLATINUM(II)+CHLORIDE'>TPT</scene></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=1b7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b7e OCA], [https://pdbe.org/1b7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b7e RCSB], [https://www.ebi.ac.uk/pdbsum/1b7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b7e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TN5P_ECOLX TN5P_ECOLX] Mediates transposition of transposon Tn5 by a 'cut and paste' mechanism. First, the monomeric transposase binds the 19 bp inverted DNA repeats flanking the transposon. Then, dimerization of the DNA-bound transposase creates a synaptic DNA complex. After nicking of the first DNA strand, excision of the transposon proceeds through a series of intermediates. The transposase then mediates the insertion of the transposon at a new site by strand transfer. The activity of the wild-type transposase is very low, and is further inhibited by dimerization with the transposase inhibitor (inh).<ref>PMID:6260374</ref> <ref>PMID:6291786</ref> <ref>PMID:6303899</ref> <ref>PMID:1310499</ref> <ref>PMID:8226636</ref> <ref>PMID:8871560</ref> <ref>PMID:11877443</ref> <ref>PMID:12367522</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Braam, L M]] | + | [[Category: Braam LM]] |
| - | [[Category: Davies, D R]] | + | [[Category: Davies DR]] |
| - | [[Category: Rayment, I]] | + | [[Category: Rayment I]] |
| - | [[Category: Reznikoff, W S]] | + | [[Category: Reznikoff WS]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Polynucleotidyl transferase]]
| + | |
| - | [[Category: Transferase inhibitor]]
| + | |
| - | [[Category: Transposase]]
| + | |
| Structural highlights
Function
TN5P_ECOLX Mediates transposition of transposon Tn5 by a 'cut and paste' mechanism. First, the monomeric transposase binds the 19 bp inverted DNA repeats flanking the transposon. Then, dimerization of the DNA-bound transposase creates a synaptic DNA complex. After nicking of the first DNA strand, excision of the transposon proceeds through a series of intermediates. The transposase then mediates the insertion of the transposon at a new site by strand transfer. The activity of the wild-type transposase is very low, and is further inhibited by dimerization with the transposase inhibitor (inh).[1] [2] [3] [4] [5] [6] [7] [8]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Transposon Tn5 employs a unique means of self-regulation by expressing a truncated version of the transposase enzyme that acts as an inhibitor. The inhibitor protein differs from the full-length transposase only by the absence of the first 55 N-terminal amino acid residues. It contains the catalytic active site of transposase and a C-terminal domain involved in protein-protein interactions. The three-dimensional structure of Tn5 inhibitor determined to 2.9-A resolution is reported here. A portion of the protein fold of the catalytic core domain is similar to the folds of human immunodeficiency virus-1 integrase, avian sarcoma virus integrase, and bacteriophage Mu transposase. The Tn5 inhibitor contains an insertion that extends the beta-sheet of the catalytic core from 5 to 9 strands. All three of the conserved residues that make up the "DDE" motif of the active site are visible in the structure. An arginine residue that is strictly conserved among the IS4 family of bacterial transposases is present at the center of the active site, suggesting a catalytic motif of "DDRE." A novel C-terminal domain forms a dimer interface across a crystallographic 2-fold axis. Although this dimer represents the structure of the inhibited complex, it provides insight into the structure of the synaptic complex.
The three-dimensional structure of a Tn5 transposase-related protein determined to 2.9-A resolution.,Davies DR, Mahnke Braam L, Reznikoff WS, Rayment I J Biol Chem. 1999 Apr 23;274(17):11904-13. PMID:10207011[9]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rothstein SJ, Reznikoff WS. The functional differences in the inverted repeats of Tn5 are caused by a single base pair nonhomology. Cell. 1981 Jan;23(1):191-9. PMID:6260374
- ↑ Johnson RC, Yin JC, Reznikoff WS. Control of Tn5 transposition in Escherichia coli is mediated by protein from the right repeat. Cell. 1982 Oct;30(3):873-82. PMID:6291786
- ↑ Lowe JB, Berg DE. A product of the TN5 transposase gene inhibits transposition. Genetics. 1983 Apr;103(4):605-15. PMID:6303899
- ↑ Wiegand TW, Reznikoff WS. Characterization of two hypertransposing Tn5 mutants. J Bacteriol. 1992 Feb;174(4):1229-39. PMID:1310499
- ↑ de la Cruz NB, Weinreich MD, Wiegand TW, Krebs MP, Reznikoff WS. Characterization of the Tn5 transposase and inhibitor proteins: a model for the inhibition of transposition. J Bacteriol. 1993 Nov;175(21):6932-8. PMID:8226636
- ↑ York D, Reznikoff WS. Purification and biochemical analyses of a monomeric form of Tn5 transposase. Nucleic Acids Res. 1996 Oct 1;24(19):3790-6. PMID:8871560
- ↑ Naumann TA, Reznikoff WS. Tn5 transposase active site mutants. J Biol Chem. 2002 May 17;277(20):17623-9. Epub 2002 Mar 4. PMID:11877443 doi:10.1074/jbc.M200742200
- ↑ Steiniger-White M, Bhasin A, Lovell S, Rayment I, Reznikoff WS. Evidence for "unseen" transposase--DNA contacts. J Mol Biol. 2002 Oct 4;322(5):971-82. PMID:12367522
- ↑ Davies DR, Mahnke Braam L, Reznikoff WS, Rayment I. The three-dimensional structure of a Tn5 transposase-related protein determined to 2.9-A resolution. J Biol Chem. 1999 Apr 23;274(17):11904-13. PMID:10207011
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