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| - | [[Image:1wth.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1wth| PDB=1wth | SCENE= }} | | {{STRUCTURE_1wth| PDB=1wth | SCENE= }} |
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| - | '''Crystal structure of gp5-S351L mutant and gp27 complex'''
| + | ===Crystal structure of gp5-S351L mutant and gp27 complex=== |
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| - | ==Overview==
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| - | Bacteriophage T4 has an efficient mechanism for injecting the host Escherichiacoli cell with genomic DNA. Its gene product 5 (gp5) has a needle-like structure attached to the end of a tube through which the DNA passes on its way out of the head and into the host. The gp5 needle punctures the outer cell membrane and then digests the peptidoglycan cell wall in the periplasmic space. gp5 is normally post-translationally cleaved between residues 351 and 352. The function of this process in controlling the lysozyme activity of gp5 has now been investigated. When gp5 is over-expressed in E.coli, two mutants (S351H and S351A) showed a reduction of cleavage products and five other mutants (S351L, S351K, S351Y, S351Q, and S351T) showed no cleavage. Furthermore, in a complementation assay at 20 degrees C, the mutants that had no cleavage of gp5 produced a reduced number of plaques compared to wild-type T4. The crystal structure of the non-cleavage phenotype mutant of gp5, S351L, complexed with gene product 27, showed that the 18 residues in the vicinity of the potential cleavage site (disordered in the wild-type structure) had visible electron density. The polypeptide around the potential cleavage site is exposed, thus allowing access for an E.coli protease. The lysozyme activity is inhibited in the wild-type structure by a loop from the adjacent gp5 monomer that binds into the substrate-binding site. The same inhibition is apparent in the mutant structure, showing that the lysozyme is inhibited before gp5 is cleaved and, presumably, the lysozyme is activated only after gp5 has penetrated the outer membrane.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15701513}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15701513 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15701513}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: T4 tail lysozyme]] | | [[Category: T4 tail lysozyme]] |
| | [[Category: Triple-stranded beta-helix]] | | [[Category: Triple-stranded beta-helix]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:06:55 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:57:05 2008'' |
Revision as of 13:57, 28 July 2008
Template:STRUCTURE 1wth
Crystal structure of gp5-S351L mutant and gp27 complex
Template:ABSTRACT PUBMED 15701513
About this Structure
1WTH is a Protein complex structure of sequences from Enterobacteria phage t4. Full crystallographic information is available from OCA.
Reference
Control of bacteriophage T4 tail lysozyme activity during the infection process., Kanamaru S, Ishiwata Y, Suzuki T, Rossmann MG, Arisaka F, J Mol Biol. 2005 Mar 4;346(4):1013-20. Epub 2005 Jan 25. PMID:15701513
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