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1ka8

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{{STRUCTURE_1ka8| PDB=1ka8 | SCENE= }}
{{STRUCTURE_1ka8| PDB=1ka8 | SCENE= }}
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'''Crystal Structure of the Phage P4 Origin-Binding Domain'''
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===Crystal Structure of the Phage P4 Origin-Binding Domain===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_11929537}}
==About this Structure==
==About this Structure==
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[[Category: Ziegelin, G.]]
[[Category: Ziegelin, G.]]
[[Category: Winged helix]]
[[Category: Winged helix]]
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Revision as of 07:01, 2 July 2008

Image:1ka8.png

Template:STRUCTURE 1ka8

Crystal Structure of the Phage P4 Origin-Binding Domain

Template:ABSTRACT PUBMED 11929537

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

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