4dm0: Difference between revisions

Latest revision as of 14:38, 14 March 2024

TN5 transposase: 20MER OUTSIDE END 2 MN complex

Structural highlights

4dm0 is a 3 chain structure with sequence from Escherichia coli. This structure supersedes the now removed PDB entries 1mur and 1l1a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	EDO, MN
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

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

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OCA

[1] 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

[2] 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

[3] Lowe JB, Berg DE. A product of the TN5 transposase gene inhibits transposition. Genetics. 1983 Apr;103(4):605-15. PMID:6303899

[4] Wiegand TW, Reznikoff WS. Characterization of two hypertransposing Tn5 mutants. J Bacteriol. 1992 Feb;174(4):1229-39. PMID:1310499

[5] 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

[6] 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

[7] 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

[8] 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

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@@ Line 1: / Line 1: @@
-[[Image:4dm0.png|left|200px]]
-{{STRUCTURE_4dm0|  PDB=4dm0  |  SCENE=  }}
+==TN5 transposase: 20MER OUTSIDE END 2 MN complex==
+<StructureSection load='4dm0' size='340' side='right'caption='[[4dm0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4dm0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mur 1mur] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1l1a 1l1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DM0 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]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=4dm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dm0 OCA], [https://pdbe.org/4dm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dm0 RCSB], [https://www.ebi.ac.uk/pdbsum/4dm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dm0 ProSAT]</span></td></tr>
+</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>
-===TN5 transposase: 20MER OUTSIDE END 2 MN complex===
+==See Also==
+*[[Transposase 3D structures|Transposase 3D structures]]
-{{ABSTRACT_PUBMED_11896402}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[4dm0]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entries  and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1l1a 1l1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DM0 OCA].
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:011896402</ref><references group="xtra"/>
 [[Category: Escherichia coli]]
-[[Category: Goryshin, I Y.]]
+[[Category: Large Structures]]
-[[Category: Klenchin, V A.]]
+[[Category: Goryshin IY]]
-[[Category: Lovell, S.]]
+[[Category: Klenchin VA]]
-[[Category: Rayment, I.]]
+[[Category: Lovell S]]
-[[Category: Reznikoff, W R.]]
+[[Category: Rayment I]]
-[[Category: Dna recombination-dna complex]]
+[[Category: Reznikoff WR]]
-[[Category: Hydrolase-dna complex]]
-[[Category: Protein-dna complex]]
-[[Category: Ribonuclease h-like motif]]
-[[Category: Synaptic complex]]
-[[Category: Transposase]]

4dm0: Difference between revisions

Latest revision as of 14:38, 14 March 2024

TN5 transposase: 20MER OUTSIDE END 2 MN complex

Structural highlights

Function

See Also

References

Contents

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