1ssw

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[[Image:1ssw.gif|left|200px]]
[[Image:1ssw.gif|left|200px]]
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{{Structure
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|PDB= 1ssw |SIZE=350|CAPTION= <scene name='initialview01'>1ssw</scene>, resolution 2.13&Aring;
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The line below this paragraph, containing "STRUCTURE_1ssw", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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{{STRUCTURE_1ssw| PDB=1ssw | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ssw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ssw OCA], [http://www.ebi.ac.uk/pdbsum/1ssw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ssw RCSB]</span>
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'''Crystal structure of phage T4 lysozyme mutant Y24A/Y25A/T26A/I27A/C54T/C97A'''
'''Crystal structure of phage T4 lysozyme mutant Y24A/Y25A/T26A/I27A/C54T/C97A'''
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[[Category: Xiao, H.]]
[[Category: Xiao, H.]]
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[[Category: bacteriolytic enzyme]]
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[[Category: Bacteriolytic enzyme]]
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[[Category: glycosidase]]
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[[Category: Glycosidase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:06:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:46:30 2008''
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Revision as of 06:06, 3 May 2008

Image:1ssw.gif

Template:STRUCTURE 1ssw

Crystal structure of phage T4 lysozyme mutant Y24A/Y25A/T26A/I27A/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

1SSW 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 Sat May 3 09:06:10 2008

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