1uaa

From Proteopedia

(Difference between revisions)

Revision as of 09:38, 29 September 2021

E. COLI REP HELICASE/DNA COMPLEX

Structural highlights

1uaa is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[REP_ECOLI] Rep helicase is a single-stranded DNA-dependent ATPase involved in DNA replication; it can initiate unwinding at a nick in the DNA. It binds to the single-stranded DNA and acts in a progressive fashion along the DNA in the 3' to 5' direction.

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

Crystal structures of binary and ternary complexes of the E. coli Rep helicase bound to single-stranded (ss) DNA or ssDNA and ADP were determined to a resolution of 3.0 A and 3.2 A, respectively. The asymmetric unit in the crystals contains two Rep monomers differing from each other by a large reorientation of one of the domains, corresponding to a swiveling of 130 degrees about a hinge region. Such domain movements are sufficiently large to suggest that these may be coupled to translocation of the Rep dimer along DNA. The ssDNA binding site involves the helicase motifs Ia, III, and V, whereas the ADP binding site involves helicase motifs I and IV. Residues in motifs II and VI may function to transduce the allosteric effects of nucleotides on DNA binding. These structures represent the first view of a DNA helicase bound to DNA.

Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP.,Korolev S, Hsieh J, Gauss GH, Lohman TM, Waksman G Cell. 1997 Aug 22;90(4):635-47. PMID:9288744^[1]

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

References

↑ Korolev S, Hsieh J, Gauss GH, Lohman TM, Waksman G. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell. 1997 Aug 22;90(4):635-47. PMID:9288744

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/1uaa"

@@ Line 3: / Line 3: @@
 <StructureSection load='1uaa' size='340' side='right'caption='[[1uaa]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1uaa]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UAA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UAA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1uaa]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UAA FirstGlance]. <br>
-</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=1uaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uaa OCA], [http://pdbe.org/1uaa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uaa RCSB], [http://www.ebi.ac.uk/pdbsum/1uaa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uaa ProSAT]</span></td></tr>
+</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=1uaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uaa OCA], [https://pdbe.org/1uaa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uaa RCSB], [https://www.ebi.ac.uk/pdbsum/1uaa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uaa ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/REP_ECOLI REP_ECOLI]] Rep helicase is a single-stranded DNA-dependent ATPase involved in DNA replication; it can initiate unwinding at a nick in the DNA. It binds to the single-stranded DNA and acts in a progressive fashion along the DNA in the 3' to 5' direction.
+[[https://www.uniprot.org/uniprot/REP_ECOLI REP_ECOLI]] Rep helicase is a single-stranded DNA-dependent ATPase involved in DNA replication; it can initiate unwinding at a nick in the DNA. It binds to the single-stranded DNA and acts in a progressive fashion along the DNA in the 3' to 5' direction.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 *[[Helicase|Helicase]]
 *[[Helicase 3D structures|Helicase 3D structures]]
-*[[Molecular Playground/PcrA Helicase|Molecular Playground/PcrA Helicase]]
-*[[PcrA helicase|PcrA helicase]]
 == References ==
 <references/>

1uaa

From Proteopedia

Revision as of 09:38, 29 September 2021

E. COLI REP HELICASE/DNA COMPLEX

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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