1t8f
From Proteopedia
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|PDB= 1t8f |SIZE=350|CAPTION= <scene name='initialview01'>1t8f</scene>, resolution 2.15Å | |PDB= 1t8f |SIZE=350|CAPTION= <scene name='initialview01'>1t8f</scene>, resolution 2.15Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span> |
| - | |GENE= E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | |GENE= E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4]) |
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t8f OCA], [http://www.ebi.ac.uk/pdbsum/1t8f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t8f RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1T8F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1T8F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T8F OCA]. |
==Reference== | ==Reference== | ||
Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation., He MM, Wood ZA, Baase WA, Xiao H, Matthews BW, Protein Sci. 2004 Oct;13(10):2716-24. Epub 2004 Aug 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15340171 15340171] | Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation., He MM, Wood ZA, Baase WA, Xiao H, Matthews BW, Protein Sci. 2004 Oct;13(10):2716-24. Epub 2004 Aug 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15340171 15340171] | ||
| - | [[Category: | + | [[Category: Enterobacteria phage t4]] |
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Wood, Z A.]] | [[Category: Wood, Z A.]] | ||
[[Category: Xiao, H.]] | [[Category: Xiao, H.]] | ||
| - | [[Category: BME]] | ||
| - | [[Category: CL]] | ||
[[Category: lysozyme]] | [[Category: lysozyme]] | ||
[[Category: poly-alanine mutation]] | [[Category: poly-alanine mutation]] | ||
[[Category: t4]] | [[Category: t4]] | ||
| - | ''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 23:52:44 2008'' |
Revision as of 20:52, 30 March 2008
| |||||||
| , resolution 2.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | E (Enterobacteria phage T4) | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of phage T4 lysozyme mutant R14A/K16A/I17A/K19A/T21A/E22A/C54T/C97A
Overview
In general, alpha-helical conformations in proteins depend in large part on the amino acid residues within the helix and their proximal interactions. For example, an alanine residue has a high propensity to adopt an alpha-helical conformation, whereas that of a glycine residue is low. The sequence preferences for beta-sheet formation are less obvious. To identify the factors that influence beta-sheet conformation, a series of scanning polyalanine mutations were made within the strands and associated turns of the beta-sheet region in T4 lysozyme. For each construct the stability of the folded protein was reduced substantially, consistent with removal of native packing interactions. However, the crystal structures showed that each of the mutants retained the beta-sheet conformation. These results suggest that the structure of the beta-sheet region of T4 lysozyme is maintained to a substantial extent by tertiary interactions with the surrounding parts of the protein. Such tertiary interactions may be important in determining the structures of beta-sheets in general.
About this Structure
1T8F is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
Reference
Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation., He MM, Wood ZA, Baase WA, Xiao H, Matthews BW, Protein Sci. 2004 Oct;13(10):2716-24. Epub 2004 Aug 31. PMID:15340171
Page seeded by OCA on Sun Mar 30 23:52:44 2008
