1ka8
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ka8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ka8 OCA], [http://www.ebi.ac.uk/pdbsum/1ka8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ka8 RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KA8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1KA8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p4 Enterobacteria phage p4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KA8 OCA]. |
==Reference== | ==Reference== | ||
Phage P4 origin-binding domain structure reveals a mechanism for regulation of DNA-binding activity by homo- and heterodimerization of winged helix proteins., Yeo HJ, Ziegelin G, Korolev S, Calendar R, Lanka E, Waksman G, Mol Microbiol. 2002 Feb;43(4):855-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11929537 11929537] | Phage P4 origin-binding domain structure reveals a mechanism for regulation of DNA-binding activity by homo- and heterodimerization of winged helix proteins., Yeo HJ, Ziegelin G, Korolev S, Calendar R, Lanka E, Waksman G, Mol Microbiol. 2002 Feb;43(4):855-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11929537 11929537] | ||
| - | [[Category: Enterobacteria phage | + | [[Category: Enterobacteria phage p4]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Calendar, R.]] | [[Category: Calendar, R.]] | ||
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[[Category: winged helix]] | [[Category: winged helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:45:37 2008'' |
Revision as of 18:45, 30 March 2008
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| , resolution 2.95Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Phage P4 Origin-Binding Domain
Overview
The origin-binding domain of the gpalpha protein of phage P4 (P4-OBD) mediates origin recognition and regulation of gpalpha activity by the protein Cnr. We have determined the crystal structure of P4-OBD at 2.95 A resolution. The structure of P4-OBD is that of a dimer with pseudo twofold symmetry. Each subunit has a winged helix topology with a unique structure among initiator proteins. The only structural homologue of the P4-OBD subunit is the DNA-binding domain of the eukaryotic transcriptional activator Rfx1. Based on this structural alignment, a model for origin recognition by the P4-OBD dimer is suggested. P4-OBD mutations that interfere with Cnr binding locate to the dimer interface, indicating that Cnr acts by disrupting the gpalpha dimer. P4-OBD dimerization is mediated by helices alpha1 and alpha3 in both subunits, a mode of winged helix protein dimerization that is reminiscent of that of the eukaryotic transcription factors E2F and DP. This, in turn, suggests that Cnr is also a winged helix protein, a possibility that is supported by previously unreported sequence homologies between Cnr and Rfx1 and homology modelling. Hence, in a mechanism that appears to be conserved from phage to man, the DNA-binding activity of winged helix proteins can be regulated by other winged helix proteins via the versatile use of the winged helix motif as a homo- or heterodimerization scaffold.
About this Structure
1KA8 is a Single protein structure of sequence from Enterobacteria phage p4. Full crystallographic information is available from OCA.
Reference
Phage P4 origin-binding domain structure reveals a mechanism for regulation of DNA-binding activity by homo- and heterodimerization of winged helix proteins., Yeo HJ, Ziegelin G, Korolev S, Calendar R, Lanka E, Waksman G, Mol Microbiol. 2002 Feb;43(4):855-67. PMID:11929537
Page seeded by OCA on Sun Mar 30 21:45:37 2008
