2reb
From Proteopedia
(New page: 200px<br /><applet load="2reb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2reb, resolution 2.3Å" /> '''THE STRUCTURE OF THE ...) |
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| - | [[Image:2reb.gif|left|200px]]<br /><applet load="2reb" size=" | + | [[Image:2reb.gif|left|200px]]<br /><applet load="2reb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2reb, resolution 2.3Å" /> | caption="2reb, resolution 2.3Å" /> | ||
'''THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER'''<br /> | '''THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the recA protein from Escherichia coli at 2.3-A | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2REB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Deleted_entry Deleted entry], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.99.37 3.4.99.37] Full crystallographic information is available from [http:// | + | 2REB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Deleted_entry Deleted entry], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.99.37 3.4.99.37] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Steitz, T | + | [[Category: Steitz, T A.]] |
| - | [[Category: Story, R | + | [[Category: Story, R M.]] |
[[Category: homologous recombination]] | [[Category: homologous recombination]] | ||
[[Category: self-cleavage stimulation]] | [[Category: self-cleavage stimulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:46:45 2008'' |
Revision as of 16:46, 21 February 2008
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THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER
Overview
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.
About this Structure
2REB is a Single protein structure of sequence from Escherichia coli. Active as Deleted entry, with EC number 3.4.99.37 Full crystallographic information is available from OCA.
Reference
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
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