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2rsl

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Revision as of 10:36, 7 July 2021

REFINEMENT OF GAMMA DELTA RESOLVASE REVEALS A STRIKINGLY FLEXIBLE MOLECULE

Structural highlights

2rsl is a 3 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. This structure supersedes the now removed PDB entry 1rsl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TNR1_ECOLI] This protein catalyzes the site-specific recombination of the transposon and also regulates its frequency of transposition.

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

BACKGROUND: gamma delta resolvase is a 20.5 kDa enzyme that catalyzes a site-specific recombination in the second step of the transposition of the gamma delta transposon and requires no cofactors other than Mg2+ for activity. Dimers of resolvase bind cooperatively to DNA at three inverted repeat sequences of differing geometry but catalyze recombination at only one site. RESULTS: The structure of the catalytic domain of gamma delta resolvase, which provides the protein-protein interactions in the synaptic complex, has been refined to an R-factor of 20% at 2.3 A resolution. The structures of the three independent monomers in the asymmetric unit are similar but not identical. Differences occur in the positions of surface loops and in the overall twist of the central beta-sheet of the molecule. The crystal also gives two independent structures for the dimeric form of the molecule, which also show significant differences in the relative orientations of their subunits. CONCLUSION: Resolvase is an unusually flexible protein. This conformational adaptability may be necessary to allow each of the 12 resolvase subunits in the synaptic complex to play a different but specific role in wrapping DNA, binding sites of differing geometry and catalyzing recombination.

Refinement of gamma delta resolvase reveals a strikingly flexible molecule.,Rice PA, Steitz TA Structure. 1994 May 15;2(5):371-84. PMID:8081753^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rice PA, Steitz TA. Refinement of gamma delta resolvase reveals a strikingly flexible molecule. Structure. 1994 May 15;2(5):371-84. PMID:8081753

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rsl"

Categories: Bacillus coli migula 1895 | Large Structures | Rice, P A | Steitz, T A | Site-specific recombinase

@@ Line 3: / Line 3: @@
 <StructureSection load='2rsl' size='340' side='right'caption='[[2rsl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2rsl]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1rsl 1rsl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RSL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2rsl]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1rsl 1rsl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RSL FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2rsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsl OCA], [http://pdbe.org/2rsl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rsl RCSB], [http://www.ebi.ac.uk/pdbsum/2rsl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rsl ProSAT]</span></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=2rsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsl OCA], [https://pdbe.org/2rsl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rsl RCSB], [https://www.ebi.ac.uk/pdbsum/2rsl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rsl ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TNR1_ECOLI TNR1_ECOLI]] This protein catalyzes the site-specific recombination of the transposon and also regulates its frequency of transposition.
+[[https://www.uniprot.org/uniprot/TNR1_ECOLI TNR1_ECOLI]] This protein catalyzes the site-specific recombination of the transposon and also regulates its frequency of transposition.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Resolvase|Resolvase]]
+*[[Resolvase 3D structures|Resolvase 3D structures]]
 == References ==
 <references/>

2rsl

From Proteopedia

Revision as of 10:36, 7 July 2021

REFINEMENT OF GAMMA DELTA RESOLVASE REVEALS A STRIKINGLY FLEXIBLE MOLECULE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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