2reb: Difference between revisions

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<StructureSection load='2reb' size='340' side='right'caption='[[2reb]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='2reb' size='340' side='right'caption='[[2reb]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2reb]] is a 1 chain structure with sequence from [https://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=2REB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2REB FirstGlance]. <br>
<table><tr><td colspan='2'>[[2reb]] 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=2REB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2REB FirstGlance]. <br>
</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=2reb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2reb OCA], [https://pdbe.org/2reb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2reb RCSB], [https://www.ebi.ac.uk/pdbsum/2reb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2reb ProSAT]</span></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]] 2.3&#8491;</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=2reb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2reb OCA], [https://pdbe.org/2reb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2reb RCSB], [https://www.ebi.ac.uk/pdbsum/2reb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2reb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/RECA_ECOLI RECA_ECOLI]] Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.[HAMAP-Rule:MF_00268]  
[https://www.uniprot.org/uniprot/RECA_ECOLI RECA_ECOLI] Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.[HAMAP-Rule:MF_00268]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2reb ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2reb ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the recA protein from Escherichia coli at 2.3-A resolution reveals a major domain that binds ADP and probably single- and double-stranded DNA. Two smaller subdomains at the N and C termini protrude from the protein and respectively stabilize a 6(1) helical polymer of protein subunits and interpolymer bundles. This polymer structure closely resembles that of recA/DNA filaments determined by electron microscopy. Mutations in recA protein that enhance coprotease, DNA-binding and/or strand-exchange activity can be explained if the interpolymer interactions in the crystal reflect a regulatory mechanism in vivo.
The structure of the E. coli recA protein monomer and polymer.,Story RM, Weber IT, Steitz TA Nature. 1992 Jan 23;355(6358):318-25. PMID:1731246<ref>PMID:1731246</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2reb" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Recombinase A|Recombinase A]]
*[[Recombinase A|Recombinase A]]
*[[3D structures of recombinase A|3D structures of recombinase A]]
*[[3D structures of recombinase A|3D structures of recombinase A]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Steitz, T A]]
[[Category: Steitz TA]]
[[Category: Story, R M]]
[[Category: Story RM]]
[[Category: Dna binding protein]]
[[Category: Homologous recombination]]
[[Category: Self-cleavage stimulation]]

Latest revision as of 12:21, 21 February 2024

THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMERTHE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER

Structural highlights

2reb is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RECA_ECOLI Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.[HAMAP-Rule:MF_00268]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2reb, resolution 2.30Å

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