1zae
From Proteopedia
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| - | [[Image:1zae.gif|left|200px]] | + | [[Image:1zae.gif|left|200px]] |
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| - | '''Solution structure of the functional domain of phi29 replication organizer p16.7c''' | + | {{Structure |
| + | |PDB= 1zae |SIZE=350|CAPTION= <scene name='initialview01'>1zae</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution structure of the functional domain of phi29 replication organizer p16.7c''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZAE is a [ | + | 1ZAE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_phage_f237 Vibrio phage f237]. This structure supersedes the now removed PDB entry 1Z61. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZAE OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the functional domain of phi29 replication organizer: insights into oligomerization and dna binding., Asensio JL, Albert A, Munoz-Espin D, Gonzalez C, Hermoso J, Villar L, Jimenez-Barbero J, Salas M, Meijer WJ, J Biol Chem. 2005 May 27;280(21):20730-9. Epub 2005 Mar 16. PMID:[http:// | + | Structure of the functional domain of phi29 replication organizer: insights into oligomerization and dna binding., Asensio JL, Albert A, Munoz-Espin D, Gonzalez C, Hermoso J, Villar L, Jimenez-Barbero J, Salas M, Meijer WJ, J Biol Chem. 2005 May 27;280(21):20730-9. Epub 2005 Mar 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15772069 15772069] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vibrio phage f237]] | [[Category: Vibrio phage f237]] | ||
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[[Category: phi-29 replication]] | [[Category: phi-29 replication]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:33:07 2008'' |
Revision as of 13:33, 20 March 2008
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Solution structure of the functional domain of phi29 replication organizer p16.7c
Overview
The Bacillus subtilis phage phi29-encoded membrane protein p16.7 is one of the few proteins involved in prokaryotic membrane-associated DNA replication that has been characterized at a functional and biochemical level. In this work we have determined both the solution and crystal structures of its dimeric functional domain, p16.7C. Although the secondary structure of p16.7C is remarkably similar to that of the DNA binding homeodomain, present in proteins belonging to a large family of eukaryotic transcription factors, the tertiary structures of p16.7C and homeodomains are fundamentally different. In fact, p16.7C defines a novel dimeric six-helical fold. We also show that p16.7C can form multimers in solution and that this feature is a key factor for efficient DNA binding. Moreover, a combination of NMR and x-ray approaches, combined with functional analyses of mutants, revealed that multimerization of p16.7C dimers is mediated by a large protein surface that is characterized by a striking self-complementarity. Finally, the structural analyses of the p16.7C dimer and oligomers provide important clues about how protein multimerization and DNA binding are coupled.
About this Structure
1ZAE is a Single protein structure of sequence from Vibrio phage f237. This structure supersedes the now removed PDB entry 1Z61. Full crystallographic information is available from OCA.
Reference
Structure of the functional domain of phi29 replication organizer: insights into oligomerization and dna binding., Asensio JL, Albert A, Munoz-Espin D, Gonzalez C, Hermoso J, Villar L, Jimenez-Barbero J, Salas M, Meijer WJ, J Biol Chem. 2005 May 27;280(21):20730-9. Epub 2005 Mar 16. PMID:15772069
Page seeded by OCA on Thu Mar 20 15:33:07 2008
